Human papilloma virus immunogen compositions and uses thereof

Abstract

Described herein is a method of preventing or treating Human Papilloma Virus (HPV) infection in a subject comprising selecting optimal HPV cytotoxic T lymphocyte (CTL) epitopes from an HPV proteome for use in a T cell immunogen composition and methods of administering the composition of subjects infected or at risk of infection with HPV.

Description

[0001]Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT HUMAN PAPILLOMA VIRUS IMMUNOGEN COMPOSITIONS AND USES THEREOF CROSS-REFERENCE TO RELATED APPLICATIONS This application claims benefit of U.S. Provisional Application No.63 / 749,872 filed on January 27, 2025, U.S. Provisional Application No.63 / 734,511 filed on December 16, 2024, and U.S. Provisional Application No.63 / 641,798 filed on May 2, 2024, the entire disclosures of which are incorporated herein by reference for any purpose. INCORPORATION BY REFERENCE STATEMENT The instant application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on May 2, 2025, is named 51506-003WO4_Sequence_Listing_5_2_25 and is 691,400 bytes in size. The vast majority of current therapeutic Human Papilloma Virus (HPV) T cell vaccines have been focused exclusively on the oncogenic E6 and E7 proteins in order to clear late-stage HPV16 / 18-driven cancers. However, such vaccines are not well designed to prevent the progression to cancer from earlier stages of neoplasia when E6 and E7 protein expression is low and other HPV proteins (E1, E2, and E5) are higher in expression. In addition, the small proteomic size of E6 and E7 limits the number of immunogenic epitopes and coverage of diverse human leukocyte antigen (HLA) populations that could be incorporated into a therapeutic HPV vaccine. One major challenge to the development of vaccines that incorporate E1, E2, and E5 is the large collective size of these proteins which can be difficult to accommodate in current T cell-inducing vaccine platforms. It would therefore be beneficial to develop vaccines that overcome these size constraints by identifying and incorporating specific immunogenic regions within the E1, E2, E5, E6, and E7 proteins from high-risk HPV strains. In addition, given the established sequence variation of HPV16, HPV18 and other high-risk strains, identification of mutation constrained T cell epitopes would also provide substantial benefit. SUMMARY Described herein are improved immunogenic compositions for use in vaccine therapies for the treatment and prevention of HPV infection. In one aspect, the invention provides a multi-epitope T cell immunogen composition comprising two or more HPV epitopes comprising a sequence from or selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to an HPV epitope in FIG.5. In one embodiment, the multi-epitope T cell immunogen composition comprises two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, wherein the HPV epitopes selected from FIG.5 are or comprise: (SEQ ID NO: 107), (SEQ ID NO: 449), (SEQ ID NO: 1), (SEQ ID NO: 2), (SEQ ID NO: 3), (SEQ ID NO: 4), (SEQ ID NO: 5), (SEQ ID NO: 6), (SEQ ID NO: 7), (SEQ ID NO: 8), (SEQ ID NO: 9), (SEQ ID NO: 10), (SEQ ID NO: 11), (SEQ ID NO: 12), (SEQ ID NO: 13), (SEQ ID NO: 14), (SEQ ID NO: 15), (SEQ ID NO: 16), (SEQ ID NO: 17), (SEQ ID NO: 18), (SEQ ID NO: 19), (SEQ ID NO: 20), (SEQ ID NO: 21), (SEQ ID NO: 22), (SEQ ID NO: 23), (SEQ ID NO: 24), (SEQ ID NO: 25), (SEQ ID NO: 26), (SEQ ID NO: 27), (SEQ ID NO: 28), (SEQ ID NO: 29), (SEQ ID NO: 30), (SEQ ID NO: 31), (SEQ ID NO: 32), (SEQ ID NO: 33), (SEQ ID NO: 34), (SEQ ID NO: 35), (SEQ ID NO: 36), (SEQ ID NO: 37), (SEQ ID NO: 38), (SEQ ID NO: 39), (SEQ ID NO: 40), (SEQ ID NO: 41), (SEQ ID NO: 42), (SEQ ID NO: 43), (SEQ ID NO: 44), (SEQ ID NO: 45), (SEQ ID NO: 46), (SEQ ID NO: 47), (SEQ ID NO: 48), (SEQ ID NO: 49), (SEQ ID NO: 50), (SEQ ID NO: 51), (SEQ ID NO: 52), (SEQ ID NO: 53), (SEQ ID NO: 54), (SEQ ID NO: 55), (SEQ ID NO: 56), (SEQ ID NO: 57), (SEQ ID NO: 58), (SEQ ID NO: 59), (SEQ ID NO: 60), (SEQ ID NO: 61), (SEQ ID NO: 62), (SEQ ID NO: 63), (SEQ ID NO: 64), (SEQ ID NO: 65), (SEQ ID NO: 66), (SEQ ID NO: 67), (SEQ ID NO: 68), (SEQ ID NO: 69), (SEQ ID NO: 70), (SEQ ID NO: 71), (SEQ ID NO: 72), (SEQ ID NO: 73), (SEQ ID NO: 74), (SEQ ID NO: 75), (SEQ ID NO: 76), (SEQ ID NO: 77), (SEQ ID NO: 78), (SEQ ID NO: 79), (SEQ ID NO: 80), (SEQ ID NO: 81), (SEQ ID NO: 82), (SEQ ID NO: 83), (SEQ ID NO: 84), (SEQ ID NO: 85), (SEQ ID NO: 86), (SEQ ID NO: 87), (SEQ ID NO: 88), (SEQ ID NO: 89), (SEQ ID NO: 90), (SEQ ID NO: 91), (SEQ ID NO: 92), (SEQ ID NO: 93), (SEQ ID NO: 94), (SEQ ID NO: 95), (SEQ ID NO: 96), (SEQ ID NO: 97), (SEQ ID NO: 98), (SEQ ID NO: 99), (SEQ ID NO: 100), (SEQ ID NO: 101), (SEQ ID NO: 102), (SEQ ID NO: 103), (SEQ ID NO: 104), (SEQ ID NO: 105), (SEQ ID NO: 106), (SEQ ID NO: 108), (SEQ ID NO: 109), (SEQ ID NO: 110), (SEQ ID NO: 111), (SEQ ID NO: 112), (SEQ ID NO: 113), (SEQ ID NO: 114), (SEQ ID NO: 115), (SEQ ID NO: 116) (SEQ ID NO: 116), (SEQ ID NO: 117), (SEQ ID NO: 118), (SEQ ID NO: 119), (SEQ ID NO: 120), (SEQ ID NO: 121), (SEQ ID NO: 122), (SEQ ID NO: 123), (SEQ ID NO: 124), (SEQ ID NO: 125), (SEQ ID NO: 126), (SEQ ID NO: 127), (SEQ ID NO: 128), (SEQ ID NO: 129), (SEQ ID NO: 130), (SEQ ID NO: 131), (SEQ ID NO: 132), (SEQ ID NO: 133), (SEQ ID NO: 134), (SEQ ID NO: 135), (SEQ ID NO: 136), (SEQ ID NO: 137), (SEQ ID NO: 138), (SEQ ID NO: 139), (SEQ ID NO: 140), (SEQ ID NO: 141), (SEQ ID NO: 142), (SEQ ID NO: 143), (SEQ ID NO: 144), (SEQ ID NO: 145), (SEQ ID NO: 146), (SEQ ID NO: 147), (SEQ ID NO: 148), (SEQ ID NO: 149), (SEQ ID NO: 150), (SEQ ID NO: 151), (SEQ ID NO: 152), (SEQ ID NO: 153), (SEQ ID NO: 154), (SEQ ID NO: 155), (SEQ ID NO: 156), (SEQ ID NO: 157), (SEQ ID NO: 158), (SEQ ID NO: 159), (SEQ ID NO: 160), (SEQ ID NO: 161), (SEQ ID NO: 162), (SEQ ID NO: 163), (SEQ ID NO: 164), (SEQ ID NO: 165), (SEQ ID NO: 166), (SEQ ID NO: 167), (SEQ ID NO: 168), (SEQ ID NO: 169) (SEQ ID NO: 170), (SEQ ID NO: 171), (SEQ ID NO: 172), (SEQ ID NO: 173), (SEQ ID NO: 174), (SEQ ID NO: 175), (SEQ ID NO: 176), (SEQ ID NO: 177), (SEQ ID NO: 178), (SEQ ID NO: 179), (SEQ ID NO: 180), (SEQ ID NO: 181), (SEQ ID NO: 182), (SEQ ID NO: 183), (SEQ ID NO: 184), (SEQ ID NO: 185), (SEQ ID NO: 186), (SEQ ID NO: 187), (SEQ ID NO: 188), (SEQ ID NO: 189), (SEQ ID NO: 190), (SEQ ID NO: 191), (SEQ ID NO: 192), (SEQ ID NO: 193), (SEQ ID NO: 194), (SEQ ID NO: 195), (SEQ ID NO: 196), (SEQ ID NO: 197), (SEQ ID NO: 198), (SEQ ID NO: 199), Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT (SEQ ID NO: 200), (SEQ ID NO: 201), (SEQ ID NO: 202), (SEQ ID NO: 203), (SEQ ID NO: 204), (SEQ ID NO: 205), (SEQ ID NO: 206), (SEQ ID NO: 207), (SEQ ID NO: 208), (SEQ ID NO: 209), (SEQ ID NO: 210), (SEQ ID NO: 211), (SEQ ID NO: 212), (SEQ ID NO: 213), (SEQ ID NO: 214), (SEQ ID NO: 215), (SEQ ID NO: 216), (SEQ ID NO: 217), (SEQ ID NO: 218), (SEQ ID NO: 219), (SEQ ID NO: 220), (SEQ ID NO: 221), (SEQ ID NO: 222), (SEQ ID NO: 223), (SEQ ID NO: 224), (SEQ ID NO: 225), (SEQ ID NO: 226), (SEQ ID NO: 227), (SEQ ID NO: 228), (SEQ ID NO: 229), (SEQ ID NO: 230), (SEQ ID NO: 231), (SEQ ID NO: 232), (SEQ ID NO: 233), (SEQ ID NO: 234), (SEQ ID NO: 235), (SEQ ID NO: 236), (SEQ ID NO: 237), (SEQ ID NO: 238), (SEQ ID NO: 239), (SEQ ID NO: 240), (SEQ ID NO: 241), (SEQ ID NO: 242), (SEQ ID NO: 243), (SEQ ID NO: 244), (SEQ ID NO: 245), (SEQ ID NO: 246), (SEQ ID NO: 247), (SEQ ID NO: 248), (SEQ ID NO: 249), (SEQ ID NO: 250), (SEQ ID NO: 251), (SEQ ID NO: 252), (SEQ ID NO: 253), (SEQ ID NO: 254), (SEQ ID NO: 255), (SEQ ID NO: 256), (SEQ ID NO: 257), (SEQ ID NO: 258), (SEQ ID NO: 259), (SEQ ID NO: 260), (SEQ ID NO: 261), (SEQ ID NO: 262), (SEQ ID NO: 263), (SEQ ID NO: 264), (SEQ ID NO: 265), (SEQ ID NO: 266), (SEQ ID NO: 267), (SEQ ID NO: 268), (SEQ ID NO: 269), (SEQ ID NO: 270), (SEQ ID NO: 271), (SEQ ID NO: 272), (SEQ ID NO: 273), (SEQ ID NO: 274), (SEQ ID NO: 275), (SEQ ID NO: 276), (SEQ ID NO: 277), (SEQ ID NO: 278), (SEQ ID NO: 279), (SEQ ID NO: 280), (SEQ ID NO: 281), (SEQ ID NO: 282), (SEQ ID NO: 283), (SEQ ID NO: 284), (SEQ ID NO: 285), (SEQ ID NO: 286), (SEQ ID NO: 287), (SEQ ID NO: 288), (SEQ ID NO: 289), (SEQ ID NO: 290), (SEQ ID NO: 291), (SEQ ID NO: 292), (SEQ ID NO: 293), (SEQ ID NO: 294), (SEQ ID NO: 295), (SEQ ID NO: 296), (SEQ ID NO: 297), (SEQ ID NO: 298), (SEQ ID NO: 299), (SEQ ID NO: 300), (SEQ ID NO: 301), (SEQ ID NO: 302), (SEQ ID NO: 303), (SEQ ID NO: 304), (SEQ ID NO: 305), (SEQ ID NO: 306), (SEQ ID NO: 307), (SEQ ID NO: 308), (SEQ ID NO: 309), (SEQ ID NO: 310), (SEQ ID NO: 311), (SEQ ID NO: 312), (SEQ ID NO: 313), (SEQ ID NO: 314), (SEQ ID NO: 315), (SEQ ID NO: 316), (SEQ ID NO: 317), (SEQ ID NO: 318), (SEQ ID NO: 319), (SEQ ID NO: 320), (SEQ ID NO: 321), (SEQ ID NO: 322), (SEQ ID NO: 323), (SEQ ID NO: 324), (SEQ ID NO: 325), (SEQ ID NO: 326), (SEQ ID NO: 327), (SEQ ID NO: 328), (SEQ ID NO: 329), (SEQ ID NO: 330), (SEQ ID NO: 331), (SEQ ID NO: 332), (SEQ ID NO: 333), (SEQ ID NO: 334), (SEQ ID NO: 335), (SEQ ID NO: 336), (SEQ ID NO: 337), (SEQ ID NO: 338), (SEQ ID NO: 339), (SEQ ID NO: 340), (SEQ ID NO: 341), (SEQ ID NO: 342), (SEQ ID NO: 343), (SEQ ID NO: 344), (SEQ ID NO: 345), (SEQ ID NO: 346), (SEQ ID NO: 347), (SEQ ID NO: 348), (SEQ ID NO: 349), (SEQ ID NO: 350), (SEQ ID NO: 351), (SEQ ID NO: 352), (SEQ ID NO: 353), (SEQ ID NO: 354), (SEQ ID NO: 355), (SEQ ID NO: 356), (SEQ ID NO: 357), (SEQ ID NO: 358), (SEQ ID NO: 359), (SEQ ID NO: 360), (SEQ ID NO: 361), (SEQ ID NO: 362), (SEQ ID NO: 363), (SEQ ID NO: 364), (SEQ ID NO: 365), (SEQ ID NO: 366), (SEQ ID NO: 367), (SEQ ID NO: 368), (SEQ ID NO: 369), (SEQ ID NO: 370), (SEQ ID NO: 371), (SEQ ID NO: 372), (SEQ ID NO: 373), (SEQ ID NO: 374), (SEQ ID NO: 375), (SEQ ID NO: 376), (SEQ ID NO: 377), (SEQ ID NO: 378), (SEQ ID NO: 379), (SEQ ID NO: 380), (SEQ ID NO: 381), (SEQ ID NO: 382), (SEQ ID NO: 383), (SEQ ID NO: 384), (SEQ ID NO: 385), (SEQ ID NO: 386), (SEQ ID NO: 387), (SEQ ID NO: 388), (SEQ ID NO: 389), (SEQ ID NO: 390), (SEQ ID NO: 391), (SEQ ID NO: 392), (SEQ ID NO: 393), (SEQ ID NO: 394), (SEQ ID NO: 395), (SEQ ID NO: 396), (SEQ ID NO: 397), (SEQ ID NO: 398), (SEQ ID NO: 399), (SEQ ID NO: 400), (SEQ ID NO: 401), (SEQ ID NO: 402), (SEQ ID NO: 403), (SEQ ID NO: 404), (SEQ ID NO: 405), (SEQ ID NO: 406), (SEQ ID NO: 407), (SEQ ID NO: 408), (SEQ ID NO: 409), (SEQ ID NO: 410), (SEQ ID NO: 411), (SEQ ID NO: 412), (SEQ ID NO: 413), (SEQ ID NO: 414), (SEQ ID NO: 415), (SEQ ID NO: 416), (SEQ ID NO: 417), (SEQ ID NO: Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 418), (SEQ ID NO: 419), (SEQ ID NO: 420), (SEQ ID NO: 421), (SEQ ID NO: 422), (SEQ ID NO: 423), (SEQ ID NO: 424), (SEQ ID NO: 425), (SEQ ID NO: 426), (SEQ ID NO: 427), (SEQ ID NO: 428), (SEQ ID NO: 429), (SEQ ID NO: 430), (SEQ ID NO: 431), (SEQ ID NO: 432), (SEQ ID NO: 433), (SEQ ID NO: 434), (SEQ ID NO: 435), (SEQ ID NO: 436), (SEQ ID NO: 437), (SEQ ID NO: 438), (SEQ ID NO: 439), (SEQ ID NO: 440), (SEQ ID NO: 441), (SEQ ID NO: 442), (SEQ ID NO: 443), (SEQ ID NO: 444), (SEQ ID NO: 445), (SEQ ID NO: 446), (SEQ ID NO: 447), (SEQ ID NO: 448), (SEQ ID NO: 450), (SEQ ID NO: 451), (SEQ ID NO: 452), (SEQ ID NO: 453), (SEQ ID NO: 454), (SEQ ID NO: 455), (SEQ ID NO: 456), (SEQ ID NO: 457), (SEQ ID NO: 458), (SEQ ID NO: 459), (SEQ ID NO: 460), (SEQ ID NO: 461), (SEQ ID NO: 462), (SEQ ID NO: 463), (SEQ ID NO: 464), (SEQ ID NO: 465), (SEQ ID NO: 466), (SEQ ID NO: 467), (SEQ ID NO: 468), (SEQ ID NO: 469), (SEQ ID NO: 470), (SEQ ID NO: 471), (SEQ ID NO: 472), (SEQ ID NO: 473), (SEQ ID NO: 474), (SEQ ID NO: 475), (SEQ ID NO: 476), (SEQ ID NO: 477), (SEQ ID NO: 478), (SEQ ID NO: 479), (SEQ ID NO: 480), (SEQ ID NO: 481), (SEQ ID NO: 482), (SEQ ID NO: 483), (SEQ ID NO: 484), (SEQ ID NO: 485), (SEQ ID NO: 486), (SEQ ID NO: 487), (SEQ ID NO: 488), (SEQ ID NO: 489), (SEQ ID NO: 490), (SEQ ID NO: 491), (SEQ ID NO: 492), and (SEQ ID NO: 493). In one embodiment, the HPV epitopes selected from FIG.5 comprise at least one immunogenic region having an amino acid sequence of or having an amino acid sequence comprising: (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 519), (SEQ ID NO: 520), (SEQ ID NO: 521), (SEQ ID NO: 522), (SEQ ID NO: 523), (SEQ ID NO: 524), (SEQ ID NO: 525), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region, and combinations thereof. In another embodiment, the combinations of immunogenic regions are selected from or comprise: i) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); ii) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT iii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iv) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); v) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vi) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); viii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: SEQ ID NO: 544), and (SEQ ID NO: 545); ix) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); x) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xii) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548) and (SEQ ID NO: 549); xiii) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT and (SEQ ID NO: 543); xiv) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xv) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xvi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xvii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xviii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xix) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); and xx) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543). In yet another embodiment, the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, are or comprise highly networked epitopes selected from Table 1. In yet another embodiment, the two or more HPV epitopes selected from Table 1 are or comprise: (SEQ ID NO: 608), (SEQ ID NO: 554), (SEQ ID NO: 609), (SEQ ID NO: 610), (SEQ ID NO: 611), (SEQ ID NO: 612), (SEQ ID NO: 613), (SEQ ID NO: 614), (SEQ ID NO: 615), (SEQ ID NO: 616), (SEQ ID NO: 617), (SEQ ID NO: 618), (SEQ ID NO: 619), (SEQ ID NO: 620), (SEQ ID NO: 619), (SEQ ID NO: 552), (SEQ ID NO: 553), (SEQ ID NO: 555), (SEQ ID NO: 556), (SEQ ID NO: 557), (SEQ ID NO: 558), (SEQ ID NO: 559), (SEQ ID NO: 10), (SEQ ID NO: 561), (SEQ ID NO: 562), (SEQ ID NO: 563), (SEQ ID NO: 564), (SEQ ID NO: 565), (SEQ ID NO: 566), (SEQ ID NO: 567), (SEQ ID NO: 568), (SEQ ID NO: 569), (SEQ ID NO: 570), (SEQ ID NO: 571), (SEQ ID NO: 572), (SEQ ID NO: 573), (SEQ ID NO: 574), (SEQ ID NO: 575), (SEQ ID NO: 576), (SEQ ID NO: 577), (SEQ ID NO: 578), (SEQ ID NO: 579), (SEQ ID NO: 580), (SEQ ID NO: 581), (SEQ ID NO: 582), (SEQ ID NO: 583), (SEQ ID NO: 584), (SEQ ID NO: 585), (SEQ ID NO: 586), (SEQ ID NO: 587), (SEQ ID NO: 588), (SEQ ID NO: 589), (SEQ ID NO: 590), (SEQ ID NO: 591), (SEQ ID NO: 592), (SEQ ID NO: 593), and (SEQ ID NO: 594). In yet another embodiment, the HPV epitopes selected from Table 1 comprise at least one immunogenic region having an amino acid sequence of or having an amino acid sequence comprising: (SEQ ID NO: 595), (SEQ ID NO: 596), (SEQ ID NO: 597), (SEQ ID NO: 598), (SEQ ID NO: 599), (SEQ ID NO: 600), (SEQ ID NO: 601), (SEQ ID NO: 581), (SEQ ID NO: 602), (SEQ ID NO: 603), (SEQ ID NO: 577), (SEQ ID NO: 605), (SEQ ID NO: 606), or (SEQ ID NO: 607) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region and combinations thereof. In another aspect, the invention provides a vector comprising a multi-epitope T cell immunogen composition comprising two or more HPV epitopes comprising a sequence from or selected from FIG.5, or variants thereof having at least about 65% to about 99% homology or 100% homology to an HPV epitope in FIG.5. In one embodiment, the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, comprise or are selected from: (SEQ ID NO: 107), (SEQ ID NO: 449), (SEQ ID NO: 1), (SEQ ID NO: 2), (SEQ ID NO: 3), (SEQ ID NO: 4), (SEQ ID NO: 5), (SEQ ID NO: 6), (SEQ ID NO: 7), (SEQ ID NO: 8), (SEQ ID NO: 9), (SEQ ID NO: 10), (SEQ ID NO: 11), (SEQ ID NO: 12), (SEQ ID NO: 13), (SEQ ID NO: 14), (SEQ ID NO: 15), (SEQ ID NO: 16), (SEQ ID NO: 17), (SEQ ID NO: 18), (SEQ ID NO: 19), (SEQ ID NO: 20) (SEQ ID NO: 21), (SEQ ID NO: 22), (SEQ ID NO: 23), (SEQ ID NO: 24), (SEQ ID NO: 25), (SEQ ID NO: 26), (SEQ ID NO: 27), (SEQ ID NO: 28), (SEQ ID NO: 29), (SEQ ID NO: 30), (SEQ ID NO: 31), (SEQ ID NO: 32), (SEQ ID NO: 33), (SEQ ID NO: 34), (SEQ ID NO: 35), (SEQ ID NO: 36), (SEQ ID NO: 37), (SEQ ID NO: 38), (SEQ ID NO: 39), (SEQ ID NO: 40), (SEQ ID NO: 41), (SEQ ID NO: 42), (SEQ ID NO: 43), (SEQ ID NO: 44), (SEQ ID NO: 45), (SEQ ID NO: 46), (SEQ ID NO: 47), (SEQ ID NO: 48), (SEQ ID NO: 49), (SEQ ID NO: 50), (SEQ ID NO: 51), (SEQ ID NO: 52), (SEQ ID NO: 53), (SEQ ID NO: 54), (SEQ ID NO: 55), (SEQ ID NO: 56), (SEQ ID NO: 57), (SEQ ID NO: 58), (SEQ ID NO: 59), (SEQ ID NO: 60), (SEQ ID NO: 61), (SEQ ID NO: 62), (SEQ ID NO: 63), (SEQ ID NO: 64), (SEQ ID NO: 65), (SEQ ID NO: 66), (SEQ ID NO: 67), (SEQ ID NO: 68), (SEQ ID NO: 69), (SEQ ID NO: 70), (SEQ ID NO: 71), (SEQ ID NO: 72), (SEQ ID NO: 73), (SEQ ID NO: 74), (SEQ ID NO: 75), (SEQ ID NO: 76), (SEQ ID NO: 77), (SEQ ID NO: 78), (SEQ ID NO: 79), (SEQ ID NO: 80), (SEQ ID NO: 81), (SEQ ID NO: 82), (SEQ ID NO: 83), (SEQ ID NO: 84), (SEQ ID NO: 85), (SEQ ID NO: 86), (SEQ ID NO: 87), (SEQ ID NO: 88), (SEQ ID NO: 89), (SEQ ID NO: 90), (SEQ ID NO: 91), (SEQ ID NO: 92), (SEQ ID NO: 93), (SEQ ID NO: 94), (SEQ ID NO: 95), (SEQ ID NO: 96), (SEQ ID NO: 97), (SEQ ID NO: 98), (SEQ ID NO: 99), (SEQ ID NO: 100), (SEQ ID NO: 101), (SEQ ID NO: 102), (SEQ ID NO: 103), (SEQ ID NO: 104), (SEQ ID NO: 105), (SEQ ID NO: 106), (SEQ ID NO: 108), (SEQ ID NO: 109), (SEQ ID NO: 110), (SEQ ID NO: 111), (SEQ ID NO: 112), (SEQ ID NO: 113), (SEQ ID NO: 114), (SEQ ID NO: 115), (SEQ ID NO: 116) (SEQ ID NO: 116), (SEQ ID NO: 117), (SEQ ID NO: 118), (SEQ ID NO: 119), (SEQ ID NO: 120), (SEQ ID NO: 121), (SEQ ID NO: 122), (SEQ ID NO: 123), (SEQ ID NO: 124), (SEQ ID NO: 125), (SEQ ID NO: 126), (SEQ ID NO: 127), (SEQ ID NO: 128), (SEQ ID NO: 129), (SEQ ID NO: 130), (SEQ ID NO: 131), (SEQ ID NO: 132), (SEQ ID NO: 133), (SEQ ID NO: 134), (SEQ ID NO: 135), (SEQ ID NO: 136), (SEQ ID NO: 137), (SEQ ID NO: 138), (SEQ ID NO: 139), (SEQ ID NO: 140), (SEQ ID NO: 141), (SEQ ID NO: 142) (SEQ ID NO: 143), (SEQ ID NO: 144), (SEQ ID NO: 145), (SEQ ID NO: 146), (SEQ ID NO: 147), (SEQ ID NO: 148), (SEQ ID NO: 149), (SEQ ID NO: 150), (SEQ ID NO: 151), (SEQ ID NO: 152), (SEQ ID NO: 153), (SEQ ID NO: 154), (SEQ ID NO: 155), (SEQ ID NO: 156), (SEQ ID NO: 157), (SEQ ID NO: 158), (SEQ ID NO: 159), (SEQ ID NO: 160), (SEQ ID NO: 161), (SEQ ID NO: 162), (SEQ ID NO: 163), (SEQ ID NO: 164), (SEQ ID NO: 165), (SEQ ID NO: 166), (SEQ ID NO: 167), (SEQ ID NO: 168), (SEQ ID NO: 169) (SEQ ID NO: 170), (SEQ ID NO: 171), (SEQ ID NO: 172), (SEQ ID NO: 173), (SEQ ID NO: 174), (SEQ ID NO: 175), (SEQ ID NO: 176), (SEQ ID NO: 177), (SEQ ID NO: 178), (SEQ ID NO: 179), (SEQ ID NO: 180), (SEQ ID NO: 181), (SEQ ID NO: 182), (SEQ ID NO: 183), (SEQ ID NO: 184), (SEQ ID NO: 185), (SEQ ID NO: 186), (SEQ ID NO: 187), (SEQ ID NO: 188), (SEQ ID NO: 189), (SEQ ID NO: 190), (SEQ ID NO: 191), (SEQ ID NO: 192), (SEQ ID NO: 193), (SEQ ID NO: Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 194), (SEQ ID NO: 195), (SEQ ID NO: 196), (SEQ ID NO: 197), (SEQ ID NO: 198), (SEQ ID NO: 199), (SEQ ID NO: 200), (SEQ ID NO: 201), (SEQ ID NO: 202), (SEQ ID NO: 203), (SEQ ID NO: 204), (SEQ ID NO: 205), (SEQ ID NO: 206), (SEQ ID NO: 207), (SEQ ID NO: 208), (SEQ ID NO: 209), (SEQ ID NO: 210), (SEQ ID NO: 211), (SEQ ID NO: 212), (SEQ ID NO: 213), (SEQ ID NO: 214), (SEQ ID NO: 215), (SEQ ID NO: 216), (SEQ ID NO: 217), (SEQ ID NO: 218), (SEQ ID NO: 219), (SEQ ID NO: 220), (SEQ ID NO: 221), (SEQ ID NO: 222), (SEQ ID NO: 223), (SEQ ID NO: 224), (SEQ ID NO: 225), (SEQ ID NO: 226), (SEQ ID NO: 227), (SEQ ID NO: 228), (SEQ ID NO: 229), (SEQ ID NO: 230), (SEQ ID NO: 231), (SEQ ID NO: 232), (SEQ ID NO: 233), (SEQ ID NO: 234), (SEQ ID NO: 235), (SEQ ID NO: 236), (SEQ ID NO: 237), (SEQ ID NO: 238), (SEQ ID NO: 239), (SEQ ID NO: 240), (SEQ ID NO: 241), (SEQ ID NO: 242), (SEQ ID NO: 243), (SEQ ID NO: 244), (SEQ ID NO: 245), (SEQ ID NO: 246), (SEQ ID NO: 247), (SEQ ID NO: 248), (SEQ ID NO: 249), (SEQ ID NO: 250), (SEQ ID NO: 251), (SEQ ID NO: 252), (SEQ ID NO: 253), (SEQ ID NO: 254), (SEQ ID NO: 255), (SEQ ID NO: 256), (SEQ ID NO: 257), (SEQ ID NO: 258), (SEQ ID NO: 259), (SEQ ID NO: 260), (SEQ ID NO: 261), (SEQ ID NO: 262), (SEQ ID NO: 263), (SEQ ID NO: 264), (SEQ ID NO: 265), (SEQ ID NO: 266), (SEQ ID NO: 267), (SEQ ID NO: 268), (SEQ ID NO: 269), (SEQ ID NO: 270), (SEQ ID NO: 271), (SEQ ID NO: 272), (SEQ ID NO: 273), (SEQ ID NO: 274), (SEQ ID NO: 275), (SEQ ID NO: 276), (SEQ ID NO: 277), (SEQ ID NO: 278), (SEQ ID NO: 279), (SEQ ID NO: 280), (SEQ ID NO: 281), (SEQ ID NO: 282), (SEQ ID NO: 283), (SEQ ID NO: 284), (SEQ ID NO: 285), (SEQ ID NO: 286), (SEQ ID NO: 287), (SEQ ID NO: 288), (SEQ ID NO: 289), (SEQ ID NO: 290), (SEQ ID NO: 291), (SEQ ID NO: 292), (SEQ ID NO: 293), (SEQ ID NO: 294), (SEQ ID NO: 295), (SEQ ID NO: 296), (SEQ ID NO: 297), (SEQ ID NO: 298), (SEQ ID NO: 299), (SEQ ID NO: 300), (SEQ ID NO: 301), (SEQ ID NO: 302), (SEQ ID NO: 303), (SEQ ID NO: 304), (SEQ ID NO: 305), (SEQ ID NO: 306), (SEQ ID NO: 307), (SEQ ID NO: 308), (SEQ ID NO: 309), (SEQ ID NO: 310), (SEQ ID NO: 311), (SEQ ID NO: 312), (SEQ ID NO: 313), (SEQ ID NO: 314), (SEQ ID NO: 315), (SEQ ID NO: 316), (SEQ ID NO: 317), (SEQ ID NO: 318), (SEQ ID NO: 319), (SEQ ID NO: 320), (SEQ ID NO: 321), (SEQ ID NO: 322), (SEQ ID NO: 323), (SEQ ID NO: 324), (SEQ ID NO: 325), (SEQ ID NO: 326), (SEQ ID NO: 327), (SEQ ID NO: 328), (SEQ ID NO: 329), (SEQ ID NO: 330), (SEQ ID NO: 331), (SEQ ID NO: 332), (SEQ ID NO: 333), (SEQ ID NO: 334), (SEQ ID NO: 335), (SEQ ID NO: 336), (SEQ ID NO: 337), (SEQ ID NO: 338), (SEQ ID NO: 339), (SEQ ID NO: 340), (SEQ ID NO: 341), (SEQ ID NO: 342), (SEQ ID NO: 343), (SEQ ID NO: 344), (SEQ ID NO: 345), (SEQ ID NO: 346), (SEQ ID NO: 347), (SEQ ID NO: 348), (SEQ ID NO: 349), (SEQ ID NO: 350), (SEQ ID NO: 351), (SEQ ID NO: 352), (SEQ ID NO: 353), (SEQ ID NO: 354), (SEQ ID NO: 355), (SEQ ID NO: 356), (SEQ ID NO: 357), (SEQ ID NO: 358), (SEQ ID NO: 359), (SEQ ID NO: 360), (SEQ ID NO: 361), (SEQ ID NO: 362), (SEQ ID NO: 363), (SEQ ID NO: 364), (SEQ ID NO: 365), (SEQ ID NO: 366), (SEQ ID NO: 367), (SEQ ID NO: 368), (SEQ ID NO: 369), (SEQ ID NO: 370), (SEQ ID NO: 371), (SEQ ID NO: 372), (SEQ ID NO: 373), (SEQ ID NO: 374), (SEQ ID NO: 375), (SEQ ID NO: 376), (SEQ ID NO: 377), (SEQ ID NO: 378), (SEQ ID NO: 379), (SEQ ID NO: 380), (SEQ ID NO: 381), (SEQ ID NO: 382), (SEQ ID NO: 383), (SEQ ID NO: 384), (SEQ ID NO: 385), (SEQ ID NO: 386), (SEQ ID NO: 387), (SEQ ID NO: 388), (SEQ ID NO: 389), (SEQ ID NO: 390), (SEQ ID NO: 391), (SEQ ID NO: 392), (SEQ ID NO: 393), (SEQ ID NO: 394), (SEQ ID NO: 395), (SEQ ID NO: 396), (SEQ ID NO: 397), (SEQ ID NO: 398), (SEQ ID NO: 399), (SEQ ID NO: 400), (SEQ ID NO: 401), (SEQ ID NO: 402), (SEQ ID NO: 403), (SEQ ID NO: 404), (SEQ ID NO: 405), (SEQ ID NO: 406), (SEQ ID NO: 407), (SEQ ID NO: 408), (SEQ ID NO: 409), (SEQ ID NO: 410), (SEQ ID NO: 411), (SEQ ID NO: 412), (SEQ Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT ID NO: 413), (SEQ ID NO: 414), (SEQ ID NO: 415), (SEQ ID NO: 416), (SEQ ID NO: 417), (SEQ ID NO: 418), (SEQ ID NO: 419), (SEQ ID NO: 420), (SEQ ID NO: 421), (SEQ ID NO: 422), (SEQ ID NO: 423), (SEQ ID NO: 424), (SEQ ID NO: 425), (SEQ ID NO: 426), (SEQ ID NO: 427), (SEQ ID NO: 428), (SEQ ID NO: 429), (SEQ ID NO: 430), (SEQ ID NO: 431), (SEQ ID NO: 432), (SEQ ID NO: 433), (SEQ ID NO: 434), (SEQ ID NO: 435), (SEQ ID NO: 436), (SEQ ID NO: 437), (SEQ ID NO: 438), (SEQ ID NO: 439), (SEQ ID NO: 440), (SEQ ID NO: 441), (SEQ ID NO: 442), (SEQ ID NO: 443), (SEQ ID NO: 444), (SEQ ID NO: 445), (SEQ ID NO: 446), (SEQ ID NO: 447), (SEQ ID NO: 448), (SEQ ID NO: 450), (SEQ ID NO: 451), (SEQ ID NO: 452), (SEQ ID NO: 453), (SEQ ID NO: 454), (SEQ ID NO: 455), (SEQ ID NO: 456), (SEQ ID NO: 457), (SEQ ID NO: 458), (SEQ ID NO: 459), (SEQ ID NO: 460), (SEQ ID NO: 461), (SEQ ID NO: 462), (SEQ ID NO: 463), (SEQ ID NO: 464), (SEQ ID NO: 465), (SEQ ID NO: 466), (SEQ ID NO: 467), (SEQ ID NO: 468), (SEQ ID NO: 469), (SEQ ID NO: 470), (SEQ ID NO: 471), (SEQ ID NO: 472), (SEQ ID NO: 473), (SEQ ID NO: 474), (SEQ ID NO: 475), (SEQ ID NO: 476), (SEQ ID NO: 477), (SEQ ID NO: 478), (SEQ ID NO: 479), (SEQ ID NO: 480), (SEQ ID NO: 481), (SEQ ID NO: 482), (SEQ ID NO: 483), (SEQ ID NO: 484), (SEQ ID NO: 485), (SEQ ID NO: 486), (SEQ ID NO: 487), (SEQ ID NO: 488), (SEQ ID NO: 489), (SEQ ID NO: 490), (SEQ ID NO: 491), (SEQ ID NO: 492), and (SEQ ID NO: 493). In yet another embodiment, the HPV epitopes selected from FIG.5 comprise at least one immunogenic region having an amino acid sequence of (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 519), (SEQ ID NO: 520), (SEQ ID NO: 521), (SEQ ID NO: 522), (SEQ ID NO: 523), (SEQ ID NO: 524), (SEQ ID NO: 525), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region, and combinations thereof. In yet another embodiment, the combinations of immunogenic regions in the vector are selected from or comprise: i) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); ii) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iv) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); v) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vi) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); viii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); ix) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); x) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xii) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT xiii) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xiv) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xv) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xvi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xvii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xviii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xix) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); and xx) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543). In yet another embodiment, the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, are or comprise highly networked epitopes selected from Table 1. In yet another embodiment, the two or more HPV epitopes selected from Table 1, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the amino acid sequence of the HPV epitope selected from Table 1, are or comprise: (SEQ ID NO: 608), (SEQ ID NO: 554), (SEQ ID NO: 609), (SEQ ID NO: 610), (SEQ ID NO: 611), (SEQ ID NO: 612), (SEQ ID NO: 613), (SEQ ID NO: 614), (SEQ ID NO: 615), (SEQ ID NO: 616), (SEQ ID NO: 617), (SEQ ID NO: 618), (SEQ ID NO: 619), (SEQ ID NO: 620), (SEQ ID NO: 619), (SEQ ID NO: 552), (SEQ ID NO: 553), (SEQ ID NO: 555), (SEQ ID NO: 556), (SEQ ID NO: 557), (SEQ ID NO: 558), (SEQ ID NO: 559), (SEQ ID NO: 10), (SEQ ID NO: 561), (SEQ ID NO: 562), (SEQ ID NO: 563), (SEQ ID NO: 564), (SEQ ID NO: 565), (SEQ ID NO: 566), (SEQ ID NO: 567), (SEQ ID NO: 568), (SEQ ID NO: 569), (SEQ ID NO: 570), (SEQ ID NO: 571), (SEQ ID NO: 572), (SEQ ID NO: 573), (SEQ ID NO: 574), (SEQ ID NO: 575), (SEQ ID NO: 576), (SEQ ID NO: 577), (SEQ ID NO: 578), (SEQ ID NO: 579), (SEQ ID NO: 580), (SEQ ID NO: 581), (SEQ ID NO: 582), (SEQ ID NO: 583), (SEQ ID NO: 584), (SEQ ID NO: 585), (SEQ ID NO: 586), (SEQ ID NO: 587), (SEQ ID NO: 588), (SEQ ID NO: 589), (SEQ ID NO: 590), (SEQ ID NO: 591), (SEQ ID NO: 592), (SEQ ID NO: 593), and (SEQ ID NO: 594). In yet another embodiment, the HPV epitopes selected from Table 1 comprise an immunogenic region having an amino acid sequence of (SEQ ID NO: 595), (SEQ ID NO: 596), (SEQ ID NO: 597), (SEQ ID NO: 598), (SEQ ID NO: 599), (SEQ ID NO: 600), (SEQ ID NO: 601), (SEQ ID NO: 581), (SEQ ID NO: 602), (SEQ ID NO: 603), (SEQ ID NO: 577), (SEQ ID NO: 605), (SEQ ID NO: 606), or (SEQ ID NO: 607) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region. In yet another embodiment, the vector comprises an endoplasmic reticulum insertion signal sequence (ERISS) and / or sequence encoding a pan HLA DR-binding epitope. In yet another embodiment, the vector comprises an enzyme cleavage site sequence. In yet another embodiment, the vector comprises enzyme cleavage site that is a furin cleavage site sequence. In yet another embodiment, the sequences encoding the epitopes in the vector are directly linked to each other. In yet another embodiment, the sequences encoding the epitope in the vector s are linked by a linker sequence. In yet another embodiment, the linker sequence in the vector comprises Alanine and Tyrosine. In yet another embodiment, the linker sequence in the vector comprises Glycine and Proline. In yet another aspect, the invention provides a pharmaceutical composition comprising any of the immunogen compositions or vectors described herein. In yet another aspect, the invention provides a method of preventing or treating an HPV infection in a subject, said method comprising administering any of the immunogen compositions or vectors described herein to the subject. In yet another aspect, the invention provides methods for determining the immunogenicity of a vector or immunogenic composition comprising two or more HPV epitopes disclosed herein by measuring the immune response in a subject after administering the vector or immunogenic composition comprising the two or more of the HPV epitopes disclosed herein to the subject. In one embodiment, the immune response is measured using an ELISpot assay. The following Detailed Description, given by way of example, but not intended to limit the invention to specific embodiments described, may be understood in conjunction with the accompanying figures, incorporated herein by reference. FIG.1A depicts a flow chart for exemplary sequence of steps for selecting regions for inclusion in a networked, mutation-constrained HPV T cell vaccine. FIG.1B depicts a flow chart for exemplary sequence of steps for selecting regions for inclusion in a broadly immunogenic HPV T cell vaccine FIG.2A – FIG.2F depict development of a deep-learning prediction algorithm for HLA class I epitopes. FIG.2A depicts datasets used for training and evaluation were curated by combining data from several previous studies as well as a recent download of the Immune Epitope Database (IEDB). Eluted ligand data were used as positives and randomly sampled decoys from Swissprot (Bairoch et al., Nucleic Acid Res 2000) served as negatives. For evaluation, data from an immunopeptidomic study involving 24 mono-allelic cell lines were used (Pyke et al., Mol Cell Proteomics 2021). To evaluate immunogenicity, five studies that measure the immunogenicity of influenza epitopes identified via mass spectrometry were used. FIG.2B and FIG.2C depict peptide length distribution of the HLA-I binders, and FIG.2D and FIG. 2E depict pie charts of the proportion of epitopes per HLA-I allele in the presentation training and evaluation datasets. All alleles with less than a one percent frequency in the dataset are denoted as Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT “other.” FIG.2F depicts that the binding module takes as input the amino acid sequences of the major histocompatibility complex (MHC) and peptide in the form: [cls] mhc [sep] pep [eos], where [cls], [sep] and [eos] are special tokens that separate the two sequences. This new sequence is fed to the ESM-2 language model, and the vector representation for the [cls] token is used to represent the complex. The ligand elution module combines the binding vector with a Long Short-term Memory model (LSTM) encoding of the peptide that includes its left and right flanks in the parent protein of origin. These combined features are then concatenated and used to compute a ligand presentation score. The model is first trained on the ligand presentation task. Then, the weights of the model are frozen and the last layer of the network is tuned. This is done on the immunogenicity training set. Finally, five models are ensembled and their average score is computed. FIG.3A – FIG.3D illustrate that MUNIS deep-learning algorithm (Wohlwend et al. Deep learning enhances the prediction of HLA class I-presented CD8+T cell epitopes in foreign pathogens.2025. Nat Mach Intell.7: 232–243) outperforms state-of-the-art predictors in classifying HLA class I binders. FIG.3A shows per allele average precision and FIG.3B shows area under the receiver operating characteristic curve (ROC-AUC) of MUNIS and prior state of the art tools MixMHCpred 2.2, NetMHCpan 4.1, and MHCflurry 2.0 on predicting eluted ligands (binders) from mass spectrometry experiments from Pyke et al. against decoy peptides (non-binders). Percentages of overlap with the training datasets of each tool across all epitopes in the presentation benchmark are shown below the plots. FIG.3C shows per allele average precision and FIG.3D shows ROC-AUC of all predictors on classifying binders versus non- binders binned by epitope length. P values for pairwise comparisons between MUNIS and each predictor were calculated using the Wilcoxon rank sums test (****: p<1e-4, not shown if p>0.1). FIG.4 is a schematic illustrating a structure-based network analysis in accordance with one implementation of the present invention. Atomic coordinates from Protein Data Bank (PDB) files (T4 Lysozyme, PDB: 2LZM) are utilized to determine inter-residue interactions using established 1) energy potentials and angle and distance thresholds and 2) distances between side-chain centers of mass. This edge-based representation of the protein is used for the application of the network centrality measures (second order degree centrality, summed node edge betweenness centrality and residue ligand proximity), as has been demonstrated in the network schematic for the central node (yellow). These values are then converted to Z-scores and summed to generate composite network scores for each amino acid residue in the protein, which is visually depicted by the size of the residue. The final output is a network-based representation of the protein on the Cα backbone of the PDB file. FIG.5 depicts HPV T cell epitopes for 40 globally prevalent HLA class I alleles, identified using the MUNIS model having a score greater than 0.95. Also listed are the Epitope Network Scores for the same. MUNIS-identified epitopes having a composite epitope network score of at least about 3.00 are highly networked and are also depicted in Table 1. FIG.6A – FIG.6C depict assessment of immunogenicity of lipid nanoparticle (LNP)-mRNA HPV16 E1-E7 fragment containing vaccines in C57Bl / 6 mice by interferon-gamma (IFN-γ) Enzyme- Linked ImmunoSpot (ELISpot). FIG.6A shows representative IFN-γ ELISpot of splenocytes from phosphate buffered saline (PBS) control and LNP-mRNA vaccinated animals following stimulation with HPV16 and HPV35 peptide pools. Each row is one representative animals from each vaccine group. FIG. 6B shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT per million splenocytes in response to the HPV16 E1, E2+E5, E7 overlapping peptide pools and optimal peptide pool. FIG.6C shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV35 E1, E6 and E7 overlapping peptide pool. FIG.7A- FIG.7C depict assessment of immunogenicity of LNP-mRNA HPV16 E1-E7 fragment containing vaccines in C57Bl / 6 mice by intracellular cytokine staining. FIG.7A shows representative intracellular cytokine staining of splenocytes from PBS control and LNP-mRNA vaccinated animals following stimulation with HPV16 and HPV35 peptide pools. Each row is one representative animals from each vaccine group. FIG.7B shows composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and Tumor Necrosis Factor alpha (TNF-α) dual positive expressing cluster of differentiation 8+(CD8+) T cells) in response to the HPV16 E1, E2+E5, E7 overlapping peptide pools and optimal peptide pool. FIG.7C shows composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+T cells) in response to the HPV35 E1, E6 and E7 overlapping peptide pool. FIG.8A – FIG.8C depict assessment of immunogenicity of LNP-mRNA HPV18 E1-E7 fragment containing vaccines in C57Bl / 6 mice by IFN-γ ELISpot. FIG.8A shows representative IFN-γ ELISpot of splenocytes from PBS control and LNP-mRNA vaccinated animals following stimulation with HPV18 and HPV45 peptide pools. Each row is one representative animals from each vaccine group. FIG.8B shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV18 E1, E6, E7 overlapping peptide pools and HPV18 E6 KI9 optimal peptide. FIG.8C shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV45 E1, E6 and E7 overlapping peptide pool. FIG.9A – FIG.9C depict assessment of immunogenicity of LNP-mRNA HPV18 E1-E7 fragment containing vaccines in C57Bl / 6 mice by intracellular cytokine staining. FIG.9A shows representative intracellular cytokine staining of splenocytes from PBS control and LNP-mRNA vaccinated animals following stimulation with HPV18 and HPV45 peptide pools. Each row is one representative animals from each vaccine group. FIG.9B shows composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+T cells) in response HPV18 E1, E6, E7 overlapping peptide pools and HPV18 E6 KI9 optimal peptide. FIG.9C shows composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+T cells) in response to the HPV45 E1, E6 and E7 overlapping peptide pool. FIG.10A and FIG.10B depict assessment of immunogenicity of Chimpanzee Adenoviral (ChAd) Vector HPV16 E1-E7 fragment containing vaccines in C57Bl / 6 mice by IFN-γ ELISpot and intracellular cytokine staining. FIG.10A shows representative IFN-γ ELISpot of splenocytes from PBS control and ChAd vaccinated animals following stimulation with HPV16 and HPV35 peptide pools. Each row is representative of a single animal from each vaccine group. FIG.10B shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV16 E1 overlapping peptide pool (left) and composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+or CD4+T cells) in response to the HPV16 E1 overlapping peptide pool (middle and right). For each graph, the Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT columns are, left to right, PBS; HPV16 E1-7 Fragments, AAY; HPV16 E1-7 Fragments, ERISS-Furin; and HPV16 / 18 E1-7 Fragments, ERISS-Furin. FIG.11A and FIG.11B depict assessment of immunogenicity of Chimpanzee Adenoviral Vector HPV18 E1-E7 fragment containing vaccines in C57Bl / 6 mice by IFN-γ ELISpot and intracellular cytokine staining. FIG.11A shows representative IFN-γ ELISpot of splenocytes from PBS control and ChAd vaccinated animals following stimulation with HPV18 and HPV45 peptide pools. Each row is representative of a single animal from each vaccine group. FIG.11B shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV18 E1 overlapping peptide pool or HPV18 E6 KI9 peptide (KCIDFYSRI; left) and composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+or CD4+T cells) in response to the HPV18 E1 overlapping peptide pool or HPV18 E6 KI9 peptide (middle and right). For each graph, the columns are, left to right, PBS; HPV18 E1- 7 Fragments, AAY; and HPV16 / 18 E1-7 Fragments, ERISS-Furin. FIG.12A and FIG.12B depict assessment of immunogenicity of LNP-mRNA HPV16 E1-E7 fragment, AAY vaccine in HLA-A*02:01 knock-in mice by IFN-γ ELISpot and intracellular cytokine staining. FIG.12A shows representative IFN-γ ELISpot of splenocytes from PBS control and LNP-mRNA vaccinated animals following stimulation with HPV16 peptide pools or individual HPV16 peptides (HPV16 E7 YMLDLQPET (SEQ ID NO: 411) or HPV16 E1 CLYLHIQSL (SEQ ID NO: 107)). Peptide pools for stimulation contained MUNIS-predicted and IEDB-deposited CD8+ T cell epitopes for HLA-A*02:01 present in the vaccine. Each row is representative of a single animal from each vaccine group. FIG.12B shows composite data of T cell reactivity as determined by IFN-γ ELISpot spot forming units (SFU) per million splenocytes in response to the HPV16 E1 or E7 HLA-A*02:01 peptide pools, or HPV16 E7 YMLDLQPET (SEQ ID NO: 411) (YT9) peptide (left) and composite data of T cell reactivity as determined by intracellular cytokine staining (percentage of IFN-γ and TNF-α dual positive expressing CD8+or CD4+T cells) in response to the HPV16 E1 or E7 HLA-A*02:01 peptide pools or HPV16 E7 YMLDLQPET (SEQ ID NO: 411) (YT9) peptide (middle and right). For each graph, the columns are, left to right, PBS; and HPV16 E1-7 Fragments, AAY. DETAILED DESCRIPTION DEFINITIONS All scientific and technical terms used in this application have meanings commonly used in the art unless otherwise specified. The definitions provided herein are to facilitate understanding of certain terms used frequently herein and are not meant to limit the scope of the application. The articles "a" and "an" are used herein to refer to one or to more than one (i.e.,to at least one) of the grammatical object of the article. By way of example, "an element" means one element or more than one element. The terms "comprise," "comprising," "include," "including," "have," and "having" are used in the inclusive, open sense, meaning that additional elements may be included. The terms "such as", "e.g.", as used herein are non-limiting and are for illustrative purposes only. "Including" and "including but not limited to" are used interchangeably. The term "or" as used herein should be understood to mean "and / or", unless the context clearly indicates otherwise. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT As used herein, the term "about" or "approximately" refers to a quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length that varies by as much as 15%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2% or 1% to a reference quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length. In one embodiment, the term "about" or "approximately" refers a range of quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length ± 15%, ± 10%, ± 9%, ± 8%, ± 7%, ± 6%, ± 5%, ± 4%, ± 3%, ± 2%, or ± 1% about a reference quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length. As used herein, “polynucleotides” or “nucleic acids” refer to a polymer of nucleotides (nucleotide monomers). Thus, nucleic acids are also referred to as polynucleotides. Nucleic acids may be or may include, for example, deoxyribonucleic acids (DNAs), ribonucleic acids (RNAs), threose nucleic acids (TNAs), glycol nucleic acids (GNAs), peptide nucleic acids (PNAs), locked nucleic acids (LNAs, including LNA having a beta-D-ribo configuration, alpha-LNA having an alpha-L-ribo configuration (a diastereomer of LNA), 2'-amino-LNA having a 2'-amino functionalization, and 2'-amino-alpha-LNA having a 2'-amino functionalization), ethylene nucleic acids, cyclohexenyl nucleic acids and / or chimeras and / or combinations thereof. The terms “polypeptide,” “peptide” and “protein” are used interchangeably herein to refer to a polymer of amino acid residues. The terms apply to amino acid polymers in which one or more amino acid residue is an analog or mimetic of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers. The term “amino acid” refers to naturally occurring and synthetic amino acids, as well as amino acid analogs and amino acid mimetics that function in a manner similar to the naturally occurring amino acids. Naturally occurring amino acids are those encoded by the genetic code, as well as those amino acids that are later modified, e.g., hydroxyproline, γ-carboxyglutamate, and O-phosphoserine. Amino acid analog refers to compounds that have the same basic chemical structure as a naturally occurring amino acid, i.e., an α-carbon that is bound to a hydrogen, a carboxyl group, an amino group, and an R group, e.g., homoserine, norleucine, methionine sulfoxide, methionine, and methyl sulfonium. Such analogs have modified R groups (e.g., norleucine) or modified peptide backbones, but retain the same basic chemical structure as a naturally occurring amino acid. As used herein, the term “epitope” comprises a peptide capable of eliciting an immune response alone or in combination with other epitopes. As used herein, “messenger RNA” or “mRNA” is any RNA that encodes a (at least one) protein (e.g., a polypeptide as described herein) and can be translated to produce the encoded protein in vitro, in vivo, in situ, or ex vivo. The skilled artisan will appreciate that, except where otherwise noted, nucleic acid sequences set forth in the instant application may recite "T"s in a representative DNA sequence but where the sequence represents RNA (e.g., mRNA), the "T"s would be substituted for "U"s. Thus, any of the DNAs disclosed and identified by a particular sequence identification number herein also disclose the corresponding RNA (e.g., mRNA) sequence complementary to the DNA, where each "T" of the DNA sequence is substituted with "U." The term “linked” or “operably linked” relates to the orientation of polynucleotide elements in a functional relationship. Operably linked means that the polynucleotide sequences being linked are Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT generally contiguous and, where necessary to join two protein coding regions, contiguous and in the same reading frame. However, since enhancers generally function when separated from the promoter by several kilobases, some polynucleotides are operably linked but not contiguous. As used herein, an “immunogen” is an amino acid sequence comprising an epitope, or multiple epitopes, that elicits a T cell response. Immunogens can be used to form a therapeutic composition, such as a vaccine to treat or prevent HPV. The term "vector" refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. Preferred vectors are those capable of one or more of, autonomous replication and expression of nucleic acids to which they are linked. Vectors capable of directing the expression of genes to which they are operatively linked are referred to herein as "expression vectors". The term "variant" refers to a single or a grouping of sequences (e.g., in an amino acid sequence) that have undergone changes as referenced against a particular species or sub- populations within a particular species due to mutations, recombination / crossover or genetic drift. Examples of types of variants include, but are not limited to: single nucleotide polymorphisms (SNPs), copy number variations (CNVs), insertions / deletions (indels), single nucleotide variant (SNVs), multiple nucleotide variants (MNVs), inversions, etc. Variants may have homology to native (unmutated) amino acid sequences, including about 65% to about 99% homology to the amino acid sequence, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the amino acid sequence. As used herein, the terms "treatment," "treating," and the like, refer to obtaining a desired pharmacologic or physiologic effect. The effect may be therapeutic in terms of a partial or complete cure for a disease or an adverse effect attributable to the disease. "Treatment," as used herein, covers any treatment of a disease in a mammal, particularly in a human, and can include inhibiting the disease or condition, i.e., arresting its development; and relieving the disease, i.e., causing regression of the disease. "Treatment," as used herein, covers both prophylactic or preventive treatment (that prevents and / or slows the development of a targeted pathologic condition or disorder) and curative, therapeutic or disease-modifying treatment. In certain embodiments, the term “treatment” can include inhibiting, attenuating or preventing the development or establishment of a HPV infection in a subject, e.g., by vaccination using a preventative vaccine including antigenic material described herein to stimulate a subject’s immune system to develop adaptive immunity to HPV. "Highly networked” refers to an epitope having a composite epitope network score of at least about 3.00. Highly networked is a quantitative description of an individual epitope based on the output from the structure-based network analysis method, which is derived from its position of the epitope within the three-dimensional structure of the HPV protein. A network score greater than a score in the range of Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT about 3.00, e.g., from about 2.90 to about 3.10 is encompassed by “highly networked” because the assignment of hydrogen atoms can differ slightly from one determination to another. "Multi-networked" is a description of a nucleic acid or protein product (i.e. a T cell immunogen) that contains 2 or more highly networked epitopes. Ranges provided herein are understood to be shorthand for all of the values within the range. For example, a range of 1 to 50 is understood to include any number, combination of numbers, or sub-range from the group consisting of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 (as well as fractions thereof unless the context clearly dictates otherwise). COMPOSITIONS AND METHODS OF THE INVENTION Described herein are methods of identifying immunogenic and mutation-constrained HPV T cell epitopes using a deep learning-based HLA class I epitope prediction algorithm referred herein as MUNIS and structure-based network analysis algorithm to methods of treating a subject in need thereof through the use of T cell-based immunogens that incorporate the identified HPV T cell epitopes. Accordingly, an aspect of the invention relates to methods of scanning the vast number of peptides in the HPV proteome to identify immunogenic HPV T cell epitopes for use in an HPV vaccine. FIG.1A illustrates one example of a method 100 for selecting epitope regions for an HPV vaccine. The method employs a deep learning-based HLA class I epitope prediction algorithm (MUNIS) which uses a bimodal architecture by jointly modeling HLA class I binding and antigen processing using a carefully curated and expanded training set for HLA class I presentation of 651,237 unique HLA class I ligands across 205 HLA class I alleles. The training dataset is composed of a collection of mass spectrometry data from immunopeptidomics experiments used in NetMHCpan 4.18, MHCFlurry 2.09and MixMHCPred 2.211training sets as well as data obtained from the Immune Epitope Database (IEDB). The eluted ligand (i.e presentation) data consists of four different datasets, using the EL data deposited in the IEDB20as well as data from the netMHCpan 4.18, MHCFlurry 2.09and MixMHCpred 2.211studies. The final dataset, after filtering out test epitopes, is composed of 651,237 positive pairs and 3,701,209 negative decoys with peptide lengths from 8 to 15. Left and right flank sequences (i.e., 5 amino acids to the left, and 5 to the right) for each peptide were fetched from the parent protein sequence annotated in the IEDB. This dataset is augmented by sampling random decoy peptides from SwissProt27at a ratio of 1:5 positive to negative (i.e., when not available a matching sequence was identified by searching the Swiss-Prot sequences using MMSeqs229). The dataset was filtered to data points where the parent protein could be identified. The source and composition of the datasets utilized are depicted in FIG.2A and the peptide length distributions of the training and evaluation datasets are depicted in FIG. 2B and FIG.2C. Sequences for the HLA alleles were obtained from the international ImMunoGeneTics information system (IMGT) database30; the model takes as input the full alpha-1 and alpha-2 domains of the HLA sequence, specifically the 180 residues ranging from positions 27 to 207. Depicted in FIG.2D and FIG. 2E are the frequencies at which peptides bind HLA molecules in the training and evaluation datasets. The model is composed of two sub-modules (FIG.2F). First, the binding module takes as input Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT the sequences of the HLA class I molecule and peptide and learns a numerical vector representation, i.e., binding features, used to produce the final prediction. The second module augments the binding features with a signal that is relevant to antigen processing. This is accomplished by an encoding of the peptide and its five N- and C- flanking residues in the parent protein of origin, like MHCFlurry 2.09. Using this approach, five models are trained and combined in an ensemble by taking their average score on any given input. The binding module uses the ESM-2 protein language model of 6 million parameters28. Language models are trained on millions of protein sequences and have been shown to implicitly learn various structural features of proteins from sequence alone. The language model takes as input the HLA & peptide sequences in the form: [CLS] HLA [SEP] PEP [EOS], where the [CLS], [SEP] and [EOS] tokens indicate the start, separator and end of the sequence respectively. After encoding the sequence with the language model, the representation of the [CLS] token was used as sequence representation, which was then fed to a two-layer feed-forward network. The loss is the binary cross entropy between the output scores and the ground truth labels. The presentation module uses a bi-directional LSTM26, which is fed the peptide sequence as a 1- hot encoded amino acids, including its left and right flanks, corresponding to 5 amino acids to the left and to the right of the peptide in its parent protein sequence of origin. To allow the network to determine which of the amino acids belong to the peptide sequence and not to the flanks, a binary feature is included at each amino acid position. The output of the LSTM is a sequence of vectors, which is pooled into a single vector representation for the sequence by averaging along the sequence length dimension. Finally, this feature vector is concatenated with the one from the binding module and fed into a 2 layer feed-forward network to produce the presentation score. Optimal HPV T cell epitopes for 40 globally prevalent HLA class I alleles, identified using the MUNIS model with a score greater than 0.95, for use in immunogenic compositions of the invention include but are not limited to those described in FIG.5, as well as variants thereof that share at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology), or at least 75% to 85% homology. Any number or combination of the epitopes identified using MUNIS, or variants thereof, can be included in an immunogenic construct of the invention, e.g., from 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 epitopes or more and / or all variants thereof. Once identified and selected, delivery of selected MUNIS-identified HPV epitopes to a subject can be accomplished through the use of an immunogenic composition. Optimal immunogenic HPV epitopes selected in accordance with a method described herein can be incorporated into a T cell-based immunogen for use in generating an effective prophylactic and therapeutic T cell vaccine for HPV. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT In other embodiments, separate computational algorithms are utilized, to identify mutation- constrained HPV T cell epitopes. In one embodiment, a structure-based network analysis algorithm employing protein structure data and network theory metrics allows for the calculation of a network score for individual amino acid residues across the HPV proteome thereby allowing for the identification of optimal mutation constrained T cell epitopes by summation of the individual amino acid residue network scores. Methods of network score analysis for identifying immunogenic epitopes of HIV and SARS-CoV-2 are known and previously published as Gaiha GD, et al. Structural topology defines protective CD8+ T cell epitopes in the HIV proteome. Science.2019 May 3;364(6439):480-484; and Nathan A, et al, Structure-guided T cell vaccine design for SARS-CoV-2 variants and sarbecoviruses. Cell.2021 Aug 19;184(17):4401-4413.e10., the contents each of which is expressly incorporated herein by reference. Accordingly, an aspect of the invention relates to a method of identifying and selecting mutation constrained HPV T cell epitopes for use in an HPV vaccine. The method employs a structure-based network analysis, which utilizes protein structure data to quantify the topological importance of each amino acid residue to a protein’s tertiary and quaternary structure. The method 100 models the relationship between residue topology and mutational tolerance by focusing on interactions made by atoms unique to an amino acid’s identity. This was accomplished by using atomic level coordinate data from the Protein Data Bank to build networks comprising nodes, representing amino acid residues, and edges, representing non- covalent interactions between the amino acid residues. These inter-residue interactions were calculated between pairs of amino acids using energy potentials and established distance thresholds and summed to generate the protein network. Using the network-based representation, an array of network centrality metrics, representing the relative importance of the various residues in a given network topology, are employed to provide a quantitative measure of the topological importance of individual amino acid residues through an assessment of their local connectivity to other residues, their involvement as bridges between higher order protein elements, such as secondary structure, tertiary and quaternary structure interfaces, and their proximity to known protein ligands. These metrics are integrated into a network score that quantifies the relative contribution of each amino acid residue to the protein’s topological structure. As depicted in FIG.4, at least one network representing protein structure is generated. An energetic approach, representing non-covalent interactions between individual atoms of amino acid residues, can be applied to generate one network. Non-covalent interactions considered in determining edge weights can include van der Waals interactions, hydrogen bonds, salt bridges, disulfide bonds, pi-pi interactions, pi-cation interactions, metal coordinated bonds and local hydrophobic packing. Each energetic protein network is then constructed by defining each individual amino acid residue within the protein structure as a node and defining weighted edges as the sum of all intermolecular bond energies between residues. Energies for each bond type were defined using previously established values in kJ / mol. The values for edges were then summed over the atoms in each amino acid residue to transform the edge list from a list of atom- atom interactions to a list of residue-residue interactions. In an example implementation, the energetic network can be filtered to consider only those edges that are between terminal atoms to provide a second network focusing on residue- specific interactions. In this network, edges within the energetic network for which neither of the two participating atoms are a terminal atom are removed. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT A centroid approach can be used to generate another network, representing the contribution of hydrophobic packing to protein folding. The centroid approach can be performed as an alternative or a supplement to the energetic approach. Each centroid network, the side chain center of mass for each amino acid residue is calculated and bonds are defined based on a distance threshold cutoff between centroids of 8.5 angstroms. Centroid protein networks were then constructed by defining each amino acid residue as a node and defining edges as binary interactions that meet the defined 8.5 angstrom threshold for centroid-to-centroid distance. Edges to immediately neighboring amino acid residues were not included in either approach due to presence of covalent peptide bonds between these residues. Next in FIG.4, a set of network parameters are calculated. A first parameter represents the involvement of the residue in bridging different higher order protein structures. In the example implementation, higher order protein structures were identified in two ways, a classical method, for example as might be generated using the publicly available software tool Stride, and a random walk approach whereby tightly connected communities are identified and distinguished. One example of this is the Walktrap algorithm. For higher order structure filters, no edges were considered between residues within the same structural motif. The first parameter can be determined as a number of second order interactions between resides from different higher order structures, using either or both of the classical method and the random walk approach to identify the higher order structures. A second order intermodular degree can be determined by determining, for each node, a number of nodes on different higher order structures within two degrees of separation of the network. This is referred to herein as the second order intermodular degree. In the example implementation, four separate values for the second order modulation degree can be determined for each node, using the three networks defined above and the two sets of secondary structure. Each second order intermodular degree value is obtained by summing, for each neighbor of the node associated with another secondary structure module, a number of edges associated with the neighboring node, with the links between the node and the secondary structure modules defined by different methods described above. If multimeric protein structure data is utilized, this metric can be considered for the multimer prior to normalization. A first value represents the second order intermodular degree for each node in the energetic network using the classically defined secondary structure. A second value represents the second order intermodular degree for each node in the energetic network, filtered to include only edges between terminal atoms, using the classically defined secondary structure. A third value represents the second order intermodular degree for each node in the centroid network using the classically defined secondary structure. A fourth value represents the second order intermodular degree for each node in the centroid network using the secondary structure defined via the random walk approach. Each of the first, second, third, and fourth values can be standardized across all nodes to provide a standardized value, and a mean value across the first, second, third, and fourth values provides an overall value representing the second order intermodular degree (SD), for each node. A node edge betweenness represents the frequency with which a node’s edges were utilized as a shortest path between all pairs of nodes in the network, weighted by edge weight. For each edge in the network bridging two nodes in different higher order structures, it is determined the number of times that the edge is used in a shortest path between a pair of nodes in the network, determined over all unique node pairs in the network as an edge betweenness. In the example implementation, the classically Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT defined secondary structure is used to define the higher order structures. Once a value is determined for each edge, the edge betweenness for each edge associated with a node can be summed to provide a betweenness value for the node. In the example implementation, this is performed for each of the energetic network and the terminal filtered energetic network to provide two betweenness values, the values are standardized across all nodes, and then averaged to provide the final node edge betweenness value (NEB). If a multimeric version of the protein exists, then the maximum node edge betweenness is taken between the monomeric and multimeric conformations. A Euclidean distance from centroid to ligand can be determined as the distance in angstroms of a residue’s centroid to the center of mass of the protein’s ligand. The centroid is defined as the center of mass of a residue’s sidechain, weighted by atomic weight. The center of mass of the ligand was calculated using all atoms. The resulting Euclidean distance (ED) from centroid to ligand is the distance between these two centers of mass, standardized across all residues. Next in FIG.4, the network parameters are combined to provide a network score for each node. In practice, each network parameter can be standardized across all nodes and combined in a weighted linear combination to provide a final network score. In the example implementation using the three network parameters described above, the final network score can be determined as: SD + NEB – ED Eq.1 Next in FIG.1B, a network score for each of a plurality of epitopes are determined as a weighted linear combination of the amino acid residues comprising the epitope. In the example implementation, the network score for each epitope is the sum of the average of the residue network scores involved in HLA binding, T cell receptor contact and five flanking residues on both the N- and C-terminus of the epitope. Finally, a set of epitopes are selected for use in the HPV vaccine based upon their network score. In one implementation, a set of epitopes with the highest network scores are selected. In another implementation, all epitopes have a network score meeting a threshold value can be utilized. It will be appreciated that the threshold value can vary with the implementation, but in the example implementation, a threshold value of 3.06 can be used, with all epitopes over that threshold being selected. In certain embodiments, the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, or about 85% to about 90% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, are highly networked HPV epitopes capable of inducing de novo cytotoxic T cell responses in the subject. These HPV epitopes having a network score of at least about 3.0 (e.g., from about 2.90 to about 3.10) can be selected from among those in Table 1: Table 1. Deep Learning Model-Generated HPV16 and HPV18 Early Protein Epitopes having a Network Score greater than 3.0. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Highly networked HPV epitopes having a network score of at least about 3.0 (e.g., from about 2.90 to about 3.10) can be selected from among variants of those epitopes in Table 1, wherein the variants thereof share at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology). Variants can include, for example, conservative mutations made to amino acids to remove highly probable splice sites when encoded into vector constructs of the invention. Any number of combinations of the highly networked epitopes, or variants thereof, can be included in an immunogenic construct of the invention, e.g., from 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 or more highly networked epitopes and / or all variants thereof. In certain embodiments, the two or more highly networked HPV epitopes selected from Table 1 are (SEQ ID NO: 608), (SEQ ID NO: 554), (SEQ ID NO: 609), (SEQ ID NO: 610), (SEQ ID NO: 611), (SEQ ID NO: 612), (SEQ ID NO: 613), (SEQ ID NO: 614), (SEQ ID NO: 615), (SEQ ID NO: 616), (SEQ ID NO: 617), (SEQ ID NO: 618), (SEQ ID NO: 619), (SEQ ID NO: 620), (SEQ ID NO: 619), (SEQ ID NO: 552), (SEQ ID NO: 553), (SEQ ID NO: 555), (SEQ ID NO: 556), (SEQ ID NO: 557), (SEQ ID NO: 558), (SEQ ID NO: 559), (SEQ ID NO: 10), (SEQ ID NO: 561), (SEQ ID NO: 562), (SEQ ID NO: 563), (SEQ ID NO: 564), (SEQ ID NO: 565), (SEQ ID NO: 566), (SEQ ID NO: 567), (SEQ ID NO: 568), (SEQ ID NO: 569), (SEQ ID NO: 570), (SEQ ID NO: 571), (SEQ ID NO: 572), (SEQ ID NO: 573), (SEQ ID NO: 574), (SEQ ID NO: 575), (SEQ ID NO: 576), (SEQ ID NO: 577), (SEQ ID NO: 578), (SEQ ID NO: 579), (SEQ ID NO: 580), (SEQ ID NO: 581), (SEQ ID NO: 582), (SEQ ID NO: 583), (SEQ ID NO: 584), (SEQ ID NO: 585), (SEQ ID NO: 586), (SEQ ID NO: 587), (SEQ ID NO: 588), (SEQ ID NO: 589), (SEQ ID NO: 590), (SEQ ID NO: 591), (SEQ ID NO: 592), (SEQ ID NO: 593), and (SEQ ID NO: 594). In some embodiments, the HPV epitopes are restricted on the surface of an antigen presenting cell by one or more HLA alleles. "Restricted by" refers to the immunologic concept of HLA restriction, whereby certain epitopes are able to bind to specific HLA class I alleles and not others, and subsequently be recognized by T cells as a combined epitope-HLA complex. The phrase “the highly networked and / or MUNIS-identified HPV epitopes that are restricted by one or more HLA alleles” indicates that a potential T cell vaccine product could include multiple highly networked epitopes and / or MUNIS-identified epitopes that bind to one HLA allele or several HLA alleles in vivo. Optimal HPV epitopes for use in immunogenic compositions of the invention can include a combination of HPV epitopes (e.g., multi-epitope T cell immunogens) identified using highly networked HPV epitopes and / or MUNIS-identified epitopes, as well as variants thereof that share at least about 65% to about 99% homology about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology). For example, any combination of optimal HPV epitopes in Table 1 and / or FIG.5, or variants thereof that share at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT about 95% homology, about 99% homology) can be used in immunogenic compositions of the invention and any number of combinations of the identified epitopes, or variants thereof, can be included in an immunogenic construct of the invention, e.g., from 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 or more highly networked epitopes and / or all variants thereof. Variants can include, for example, conservative mutations made to amino acids to remove highly probable splice sites when encoded into vector constructs of the invention. In certain embodiments, the multi-epitope T cell immunogen composition of the invention comprises two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the selected HPV epitope, wherein the HPV epitopes selected from FIG.5 are (SEQ ID NO: 107), (SEQ ID NO: 449), (SEQ ID NO: 1), (SEQ ID NO: 2), (SEQ ID NO: 3), (SEQ ID NO: 4), (SEQ ID NO: 5), (SEQ ID NO: 6), (SEQ ID NO: 7), (SEQ ID NO: 8), (SEQ ID NO: 9), (SEQ ID NO: 10), (SEQ ID NO: 11), (SEQ ID NO: 12), (SEQ ID NO: 13), (SEQ ID NO: 14), (SEQ ID NO: 15), (SEQ ID NO: 16), (SEQ ID NO: 17), (SEQ ID NO: 18), (SEQ ID NO: 19), (SEQ ID NO: 20), (SEQ ID NO: 21), (SEQ ID NO: 22), (SEQ ID NO: 23), (SEQ ID NO: 24), (SEQ ID NO: 25), (SEQ ID NO: 26), (SEQ ID NO: 27), (SEQ ID NO: 28), (SEQ ID NO: 29), (SEQ ID NO: 30), (SEQ ID NO: 31), (SEQ ID NO: 32), (SEQ ID NO: 33), (SEQ ID NO: 34), (SEQ ID NO: 35), (SEQ ID NO: 36), (SEQ ID NO: 37), (SEQ ID NO: 38), (SEQ ID NO: 39), (SEQ ID NO: 40), (SEQ ID NO: 41), (SEQ ID NO: 42), (SEQ ID NO: 43), (SEQ ID NO: 44), (SEQ ID NO: 45), (SEQ ID NO: 46), (SEQ ID NO: 47), (SEQ ID NO: 48), (SEQ ID NO: 49), (SEQ ID NO: 50), (SEQ ID NO: 51), (SEQ ID NO: 52), (SEQ ID NO: 53), (SEQ ID NO: 54), (SEQ ID NO: 55), (SEQ ID NO: 56), (SEQ ID NO: 57), (SEQ ID NO: 58), (SEQ ID NO: 59), (SEQ ID NO: 60), (SEQ ID NO: 61), (SEQ ID NO: 62), (SEQ ID NO: 63), (SEQ ID NO: 64), (SEQ ID NO: 65), (SEQ ID NO: 66), (SEQ ID NO: 67), (SEQ ID NO: 68), (SEQ ID NO: 69), (SEQ ID NO: 70), (SEQ ID NO: 71), (SEQ ID NO: 72), (SEQ ID NO: 73), (SEQ ID NO: 74), (SEQ ID NO: 75), (SEQ ID NO: 76), (SEQ ID NO: 77), (SEQ ID NO: 78), (SEQ ID NO: 79), (SEQ ID NO: 80), (SEQ ID NO: 81), (SEQ ID NO: 82), (SEQ ID NO: 83), (SEQ ID NO: 84), (SEQ ID NO: 85), (SEQ ID NO: 86), (SEQ ID NO: 87), (SEQ ID NO: 88), (SEQ ID NO: 89), (SEQ ID NO: 90), (SEQ ID NO: 91), (SEQ ID NO: 92), (SEQ ID NO: 93), (SEQ ID NO: 94), (SEQ ID NO: 95), (SEQ ID NO: 96), (SEQ ID NO: 97), (SEQ ID NO: 98), (SEQ ID NO: 99), (SEQ ID NO: 100), (SEQ ID NO: 101), (SEQ ID NO: 102), (SEQ ID NO: 103), (SEQ ID NO: 104), (SEQ ID NO: 105), (SEQ ID NO: 106), (SEQ ID NO: 108), (SEQ ID NO: 109), (SEQ ID NO: 110), (SEQ ID NO: 111), (SEQ ID NO: 112), (SEQ ID NO: 113), (SEQ ID NO: 114), (SEQ ID NO: 115), (SEQ ID NO: 116) (SEQ ID NO: 116), (SEQ ID NO: 117), (SEQ ID NO: 118), (SEQ ID NO: 119), (SEQ ID NO: 120), (SEQ ID NO: 121), (SEQ ID NO: 122), (SEQ ID NO: 123), (SEQ ID NO: 124), (SEQ ID NO: 125), (SEQ ID NO: 126), (SEQ ID NO: 127), (SEQ ID NO: 128), Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT (SEQ ID NO: 129), (SEQ ID NO: 130), (SEQ ID NO: 131), (SEQ ID NO: 132), (SEQ ID NO: 133), (SEQ ID NO: 134), (SEQ ID NO: 135), (SEQ ID NO: 136), (SEQ ID NO: 137), (SEQ ID NO: 138), (SEQ ID NO: 139), (SEQ ID NO: 140), (SEQ ID NO: 141), (SEQ ID NO: 142), (SEQ ID NO: 143), (SEQ ID NO: 144), (SEQ ID NO: 145), (SEQ ID NO: 146), (SEQ ID NO: 147), (SEQ ID NO: 148), (SEQ ID NO: 149), (SEQ ID NO: 150), (SEQ ID NO: 151), (SEQ ID NO: 152), (SEQ ID NO: 153), (SEQ ID NO: 154), (SEQ ID NO: 155), (SEQ ID NO: 156), (SEQ ID NO: 157), (SEQ ID NO: 158), (SEQ ID NO: 159), (SEQ ID NO: 160), (SEQ ID NO: 161), (SEQ ID NO: 162), (SEQ ID NO: 163), (SEQ ID NO: 164), (SEQ ID NO: 165), (SEQ ID NO: 166), (SEQ ID NO: 167), (SEQ ID NO: 168), (SEQ ID NO: 169) (SEQ ID NO: 170), (SEQ ID NO: 171), (SEQ ID NO: 172), (SEQ ID NO: 173), (SEQ ID NO: 174), (SEQ ID NO: 175), (SEQ ID NO: 176), (SEQ ID NO: 177), (SEQ ID NO: 178), (SEQ ID NO: 179), (SEQ ID NO: 180), (SEQ ID NO: 181), (SEQ ID NO: 182), (SEQ ID NO: 183), (SEQ ID NO: 184), (SEQ ID NO: 185), (SEQ ID NO: 186), (SEQ ID NO: 187), (SEQ ID NO: 188), (SEQ ID NO: 189), (SEQ ID NO: 190), (SEQ ID NO: 191), (SEQ ID NO: 192), (SEQ ID NO: 193), (SEQ ID NO: 194), (SEQ ID NO: 195), (SEQ ID NO: 196), (SEQ ID NO: 197), (SEQ ID NO: 198), (SEQ ID NO: 199), (SEQ ID NO: 200), (SEQ ID NO: 201), (SEQ ID NO: 202), (SEQ ID NO: 203), (SEQ ID NO: 204), (SEQ ID NO: 205), (SEQ ID NO: 206), (SEQ ID NO: 207), (SEQ ID NO: 208), (SEQ ID NO: 209), (SEQ ID NO: 210), (SEQ ID NO: 211), (SEQ ID NO: 212), (SEQ ID NO: 213), (SEQ ID NO: 214), (SEQ ID NO: 215), (SEQ ID NO: 216), (SEQ ID NO: 217), (SEQ ID NO: 218), (SEQ ID NO: 219), (SEQ ID NO: 220), (SEQ ID NO: 221), (SEQ ID NO: 222), (SEQ ID NO: 223), (SEQ ID NO: 224), (SEQ ID NO: 225), (SEQ ID NO: 226), (SEQ ID NO: 227), (SEQ ID NO: 228), (SEQ ID NO: 229), (SEQ ID NO: 230), (SEQ ID NO: 231), (SEQ ID NO: 232), (SEQ ID NO: 233), (SEQ ID NO: 234), (SEQ ID NO: 235), (SEQ ID NO: 236), (SEQ ID NO: 237), (SEQ ID NO: 238), (SEQ ID NO: 239), (SEQ ID NO: 240), (SEQ ID NO: 241), (SEQ ID NO: 242), (SEQ ID NO: 243), (SEQ ID NO: 244), (SEQ ID NO: 245), (SEQ ID NO: 246), (SEQ ID NO: 247), (SEQ ID NO: 248), (SEQ ID NO: 249), (SEQ ID NO: 250), (SEQ ID NO: 251), (SEQ ID NO: 252), (SEQ ID NO: 253), (SEQ ID NO: 254), (SEQ ID NO: 255), (SEQ ID NO: 256), (SEQ ID NO: 257), (SEQ ID NO: 258), (SEQ ID NO: 259), (SEQ ID NO: 260), (SEQ ID NO: 261), (SEQ ID NO: 262), (SEQ ID NO: 263), (SEQ ID NO: 264), (SEQ ID NO: 265), (SEQ ID NO: 266), (SEQ ID NO: 267), (SEQ ID NO: 268), (SEQ ID NO: 269), (SEQ ID NO: 270), (SEQ ID NO: 271), (SEQ ID NO: 272), (SEQ ID NO: 273), (SEQ ID NO: 274), (SEQ ID NO: 275), (SEQ ID NO: 276), (SEQ ID NO: 277), (SEQ ID NO: 278), (SEQ ID NO: 279), (SEQ ID NO: 280), (SEQ ID NO: 281), (SEQ ID NO: 282), (SEQ ID NO: 283), (SEQ ID NO: 284), (SEQ ID NO: 285), (SEQ ID NO: 286), (SEQ ID NO: 287), (SEQ ID NO: 288), (SEQ ID NO: 289), (SEQ ID NO: 290), (SEQ ID NO: 291), (SEQ ID NO: 292), (SEQ ID NO: 293), (SEQ ID NO: 294), (SEQ ID NO: 295), (SEQ ID NO: 296), (SEQ ID NO: 297), (SEQ ID NO: 298), (SEQ ID NO: 299), (SEQ ID NO: 300), (SEQ ID NO: 301), (SEQ ID NO: 302), (SEQ ID NO: 303), (SEQ ID NO: 304), (SEQ ID NO: 305), (SEQ ID NO: 306), (SEQ ID NO: 307), (SEQ ID NO: 308), (SEQ ID NO: 309), (SEQ ID NO: 310), (SEQ ID NO: 311), (SEQ ID NO: 312), (SEQ ID NO: 313), (SEQ ID NO: 314), (SEQ ID NO: 315), (SEQ ID NO: 316), (SEQ ID NO: 317), (SEQ ID NO: 318), (SEQ ID NO: 319), (SEQ ID NO: 320), (SEQ ID NO: 321), (SEQ ID NO: 322), (SEQ ID NO: 323), (SEQ ID NO: 324), (SEQ ID NO: 325), (SEQ ID NO: 326), (SEQ ID NO: 327), (SEQ ID NO: 328), (SEQ ID NO: 329), (SEQ ID NO: 330), (SEQ ID NO: 331), (SEQ ID NO: 332), (SEQ ID NO: 333), (SEQ ID NO: 334), (SEQ ID NO: 335), (SEQ ID NO: 336), (SEQ ID NO: 337), (SEQ ID NO: 338), (SEQ ID NO: 339), (SEQ ID NO: 340), (SEQ ID NO: 341), (SEQ ID NO: 342), (SEQ ID NO: 343), (SEQ ID NO: 344), (SEQ ID NO: 345), (SEQ ID NO: 346), (SEQ ID NO: Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 347), (SEQ ID NO: 348), (SEQ ID NO: 349), (SEQ ID NO: 350), (SEQ ID NO: 351), (SEQ ID NO: 352), (SEQ ID NO: 353), (SEQ ID NO: 354), (SEQ ID NO: 355), (SEQ ID NO: 356), (SEQ ID NO: 357), (SEQ ID NO: 358), (SEQ ID NO: 359), (SEQ ID NO: 360), (SEQ ID NO: 361), (SEQ ID NO: 362), (SEQ ID NO: 363), (SEQ ID NO: 364), (SEQ ID NO: 365), (SEQ ID NO: 366), (SEQ ID NO: 367), (SEQ ID NO: 368), (SEQ ID NO: 369), (SEQ ID NO: 370), (SEQ ID NO: 371), (SEQ ID NO: 372), (SEQ ID NO: 373), (SEQ ID NO: 374), (SEQ ID NO: 375), (SEQ ID NO: 376), (SEQ ID NO: 377), (SEQ ID NO: 378), (SEQ ID NO: 379), (SEQ ID NO: 380), (SEQ ID NO: 381), (SEQ ID NO: 382), (SEQ ID NO: 383), (SEQ ID NO: 384), (SEQ ID NO: 385), (SEQ ID NO: 386), (SEQ ID NO: 387), (SEQ ID NO: 388), (SEQ ID NO: 389), (SEQ ID NO: 390), (SEQ ID NO: 391), (SEQ ID NO: 392), (SEQ ID NO: 393), (SEQ ID NO: 394), (SEQ ID NO: 395), (SEQ ID NO: 396), (SEQ ID NO: 397), (SEQ ID NO: 398), (SEQ ID NO: 399), (SEQ ID NO: 400), (SEQ ID NO: 401), (SEQ ID NO: 402), (SEQ ID NO: 403), (SEQ ID NO: 404), (SEQ ID NO: 405), (SEQ ID NO: 406), (SEQ ID NO: 407), (SEQ ID NO: 408), (SEQ ID NO: 409), (SEQ ID NO: 410), (SEQ ID NO: 411), (SEQ ID NO: 412), (SEQ ID NO: 413), (SEQ ID NO: 414), (SEQ ID NO: 415), (SEQ ID NO: 416), (SEQ ID NO: 417), (SEQ ID NO: 418), (SEQ ID NO: 419), (SEQ ID NO: 420), (SEQ ID NO: 421), (SEQ ID NO: 422), (SEQ ID NO: 423), (SEQ ID NO: 424), (SEQ ID NO: 425), (SEQ ID NO: 426), (SEQ ID NO: 427), (SEQ ID NO: 428), (SEQ ID NO: 429), (SEQ ID NO: 430), (SEQ ID NO: 431), (SEQ ID NO: 432), (SEQ ID NO: 433), (SEQ ID NO: 434), (SEQ ID NO: 435), (SEQ ID NO: 436), (SEQ ID NO: 437), (SEQ ID NO: 438), (SEQ ID NO: 439), (SEQ ID NO: 440), (SEQ ID NO: 441), (SEQ ID NO: 442), (SEQ ID NO: 443), (SEQ ID NO: 444), (SEQ ID NO: 445), (SEQ ID NO: 446), (SEQ ID NO: 447), (SEQ ID NO: 448), (SEQ ID NO: 450), (SEQ ID NO: 451), (SEQ ID NO: 452), (SEQ ID NO: 453), (SEQ ID NO: 454), (SEQ ID NO: 455), (SEQ ID NO: 456), (SEQ ID NO: 457), (SEQ ID NO: 458), (SEQ ID NO: 459), (SEQ ID NO: 460), (SEQ ID NO: 461), (SEQ ID NO: 462), (SEQ ID NO: 463), (SEQ ID NO: 464), (SEQ ID NO: 465), (SEQ ID NO: 466), (SEQ ID NO: 467), (SEQ ID NO: 468), (SEQ ID NO: 469), (SEQ ID NO: 470), (SEQ ID NO: 471), (SEQ ID NO: 472), (SEQ ID NO: 473), (SEQ ID NO: 474), (SEQ ID NO: 475), (SEQ ID NO: 476), (SEQ ID NO: 477), (SEQ ID NO: 478), (SEQ ID NO: 479), (SEQ ID NO: 480), (SEQ ID NO: 481), (SEQ ID NO: 482), (SEQ ID NO: 483), (SEQ ID NO: 484), (SEQ ID NO: 485), (SEQ ID NO: 486), (SEQ ID NO: 487), (SEQ ID NO: 488), (SEQ ID NO: 489), (SEQ ID NO: 490), (SEQ ID NO: 491), (SEQ ID NO: 492), and (SEQ ID NO: 493). Combinations of highly networked HPV epitopes and / or HPV epitopes identified using MUNIS can comprise the HPV immunogenic regions described in Table 2, or variants thereof that share at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology). Table 2. Immunogenic regions comprised of MUNIS-Identified epitopes. Fragments of both MUNIS-Identified and Networked Epitopes Shown in Bold and Italics. Underlines denote conservative Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT mutations made to amino acids to remove highly probable splice sites (e.g., Q > N or V > I). Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Combinations of highly networked HPV epitopes and / or HPV epitopes can comprise the HPV immunogenic regions described in Table 3. Table 3. All epitope sequences with their HPV origins Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Accordingly, in certain embodiments, a combination of HPV epitopes selected from Table 1 comprise at least one immunogenic region depicted in Table 2, having an amino acid sequence of (SEQ ID NO: 595), (SEQ ID NO: 596), (SEQ ID NO: 597), (SEQ ID NO: 598), (SEQ ID NO: 599), (SEQ ID NO: 600), (SEQ ID NO: 601), (SEQ ID NO: 581), (SEQ ID NO: 602), (SEQ ID NO: 603), (SEQ ID NO: 577), (SEQ ID NO: 605), (SEQ ID NO: 606), or (SEQ ID NO: 607) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region and combinations thereof. In other embodiments, a combination of HPV epitopes selected from FIG.5 comprise at least one immunogenic region depicted in Table 2 having an amino acid sequence of (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 519), (SEQ ID NO: 520), (SEQ ID NO: 521), (SEQ ID NO: 522), (SEQ ID NO: 523), (SEQ ID NO: 524), (SEQ ID NO: 525), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543) or variants thereof having at least about 65% to about 99% homology, about 70% to about 99% homology, about 75% to about 99% homology, about 80% to about 99% homology, about 85% to about 99% homology, about 90% to about 99% homology, about 65% to about 95% homology, about 70% to about 95% homology, about 75% to about 95% homology, about 80% to about 95% homology, about 85% to about 95% homology, about 90% to about 95% homology, about 65% to about 90% homology, about 70% to about 90% homology, about 75% to about 90% homology, about 80% to about 90% homology, about 85% to about 90% homology, or at least 75% to 85% homology (e.g., about 65% homology, about 70% homology, about 75% homology, about 80% homology, about 85% homology, about 90% homology, about 95% homology, about 99% homology) to the immunogenic region, and combinations thereof. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Multiple combinations of the immunogenic regions depicted in Table 2 can also comprise an HPV immunogenic composition of the invention. In certain embodiments, the combinations of immunogenic regions are selected from: i) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); ii) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iv) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); v) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vi) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); viii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); ix) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); x) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xii) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xiii) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xiv) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xv) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xvi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xvii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and VESSADDLRAFQQLFLNTLSFV (SEQ ID NO: 543); xviii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xix) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); and xx) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543). Methods of treating a subject for HPV infection are also provided. The methods can comprise administering to the subject an immunogenic composition including optimal HPV epitopes, wherein the optimal HPV epitopes have been identified and selected using a structure- based network analysis and / or MUNIS analysis as described above. Once identified, delivery of selected optimal HPV epitopes to a subject is accomplished through the administration of the immunogenic composition or a delivery vehicle comprising the immunogenic composition (e.g., a vector expressing the immunogenic composition). In some embodiments, an immunogenic composition for use in an HPV vaccine can include a recombinant vector including a nucleic acid sequence encoding optimal HPV epitopes. In some embodiments, an immunogenic composition for use in an HPV vaccine can include a recombinant vector including any one of the nucleic acid constructs listed in Table 4 and Table 5. Table 4. List of T cell vaccine cassettes. Target Size Size Construct Name Strain(s) (Base pairs) (Amino Acids) 16 E2, E6, E7 Fragments – ERISS Furin Cassette 1923 638 – *Note that amino acid size and nucleotide size are off by 9 bp due to exclusion of Kozak sequence and stop codons from amino acid size. Table 5. List of T cell vaccine cassettes and composition of protein fragments. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Construct Name Fragment Composition 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, E6, E7 Fragments – 16E2 F7, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, ERISS Furin Cassette 16E7 F3 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, E5, E6, E7 Fragments – 16E2 F7, 16E5 F1, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, ERISS Furin Cassette 16E7 F2, 16E7 F3 16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, E1, E2, E5, E6, E7 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, – ERISS Furin 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 F1, Cassette 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, 16E7 F3 16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, E1, E2, E5 Fragments; E6, 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, 16 E7 Full Proteins – ERISS 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 Furin Cassette Mutant, 16E7 Mutant E2, E6, E7 Fragments – 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, 16 16E2 F7, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, Cassette 16E7 F3 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, E2, E5, E6, E7 Fragments – 16 16E2 F7, 16E5 F1, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, AAY Cassette 16E7 F2, 16E7 F3 16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, E1, E2, E5, E6, E7 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, 16 Fragments – AAY Cassette 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, 16E7 F3 16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, E1, E2, E5 Fragments; E6, 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, 16 E7 Full Proteins – AAY 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 Cassette Mutant, 16E7 Mutant E2, E6, E7 Fragments – 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18E2 F5, 18E6 F1, 18 ERISS Furin Cassette 18E6 F2 18E6 F3 18E7 F1 18E7 F2 18E7 F3 18 E2, E5, E6, E7 Fragments – 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18E2 F5, 18E5 F1, ERISS Furin Cassette 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3 18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, E1, E2, E5, E6, E7 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18 Fragments – ERISS Furin 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, Cassette 18E7 F2, 18E7 F3 E1, E2, E5 Fragments; E6, 18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, 18 E7 Full Proteins – ERISS 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, Furin Cassette 18E2 F5, 18E5 F1, 18E6 Mutant, 18E7 Mutant E2, E6, E7 Fragments – AAY 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18E2 F5, 18E6 F1, 18 Cassette 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3 E2, E5, E6, E7 Fragments – 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18E2 F5, 18E5 F1, 18 AAY Cassette 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3 18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, E1, E2, E5, E6, E7 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18 Fragments – AAY Cassette 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3 E1, E2, E5 Fragments; E6, 18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, E7 Full Proteins – AAY 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, Cassette 18E2 F5, 18E5 F1, 18E6 Mutant, 18E7 Mutant 16E1 F1, 16E1 F2, 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, E1 Highly Networked; E2, 16E2 F5, 16E2 F6.2, 16E5 F1, 16E6 F1, 16E6 F2.2, 16E6 16 / 18 E5, E6, E7 Fragments – F3, 16E7 F1, 16E7 F2.2, 16E7 F3.2, 18E1 F1.2, 18E1 F2.2, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 F4, 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3 Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT The optimal HPV epitopes can be linked directly to one another with a linker. In some implementations, in some aspects, the linker is selected from the group consisting of: (1) consecutive glycine residues, at least 2, 3, 4, 5, 6, 7, 8, 9, or 10 residues in length; (2) consecutive alanine residues, at least 2, 3, 4, 5, 6, 7, 8, 9, or 10 residues in length;(3) two arginine residues (RR); (4) alanine, alanine, tyrosine (AAY); (5) a consensus sequence at least 2, 3, 4, 5, 6, 7, 8 , 9, or 10 amino acid residues in length that is processed efficiently by a mammalian proteasome; and (6) one or more native sequences flanking the antigen derived from the cognate protein of origin and that is at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, or 2-20 amino acid residues in length. In some implementations, the linker comprises the sequence GPGPG (SEQ ID NO: 656). The HPV epitopes described herein can be linked, operably or directly, to a separate or contiguous sequence that enhances the expression, stability, cell trafficking, processing and presentation, and / or immunogenicity of the epitope. The HPV sequence may include at least one of: an immunoglobulin signal sequence (e.g., immunoglobulin kappa (IgK)), a major histocompatibility class I sequence, lysosomal-associated membrane protein (LAMP)- l, human dendritic cell lysosomal-associated membrane protein, and a major histocompatibility class II sequence. In other implementations, at least one HPV epitope is linked, operably or directly, to a separate or contiguous sequence that enhances the expression, stability, cell trafficking, processing and presentation, and / or immunogenicity of the plurality. The separate or contiguous sequence can comprise at least one of: a ubiquitin sequence, a ubiquitin sequence modified to increase proteasome targeting (e.g., the ubiquitin sequence contains a Gly to Ala substitution at position 76 or Gly to Val substitution at position 76), an immunoglobulin signal sequence (e.g., IgK), a major histocompatibility class I sequence, lysosomal-associated membrane protein (LAMP)- l , human dendritic cell lysosomal-associated membrane protein, and a major histocompatibility class II sequence; optionally wherein the ubiquitin sequence modified to increase proteasome targeting is A76 or V76. The optimal HPV epitopes may be delivered to and expressed in a subject’s cells by incorporating a nucleic acid encoding two or more optimal HPV epitopes into an expression vector. As used herein, "expression vector" refers to a vector that comprises a recombinant polynucleotide including expression control sequences operatively linked to a nucleotide sequence to be expressed. An Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT expression vector comprises sufficient cis-acting elements for expression; other elements for expression can be supplied by the host cell or in an in vitro expression system. In some implementations, a recombinant expression vector can include additional immune-enhancer elements to increase epitope expression and / or de novo cytotoxic T cell responses in a subject. Immune-enhancer elements can include, but are not limited to, endoplasmic reticulum signal sequences to promote HLA class I presentation, sequences encoding a furin cleavage site (e.g., RRKR (SEQ ID NO: 654), RGRRKRS (SEQ ID NO: 655)), and / or a universal T-helper epitope such as a pan HLA-DR epitope or tetanus-diptheria (TpD) helper epitope. In some embodiments, nucleic acid molecules encoding HPV epitopes provided herein include codon-optimized sequences. As used herein, the term “codon-optimized” means a polynucleotide, nucleic acid sequence, or coding sequence has been redesigned as compared to a wild-type or reference polynucleotide, nucleic acid sequence, or coding sequence by choosing different codons without altering the amino acid sequence of the encoded protein. Accordingly, codon-optimization generally refers to replacement of codons with synonymous codons to optimize expression of a protein while keeping the amino acid sequence of the translated protein the same. Codon optimization of a sequence can increase protein expression levels (Gustafsson et al., Codon bias and heterologous protein expression.2004, Trends Biotechnol 22: 346-53) of the encoded proteins, for example, and provide other advantages. Variables such as codon usage preference as measured by codon adaptation index (CAI), for example, the presence or frequency of U and other nucleotides, mRNA secondary structures, cis-regulatory sequences, GC content, and other variables may correlate with protein expression levels (Villalobos et al., Gene Designer: a synthetic biology tool for constructing artificial DNA segments.2006, BMC Bioinformatics 7:285). Any method of codon optimization can be used to codon optimize nucleic acid molecules encoding HPV epitopes provided herein, and any variable can be altered by codon optimization. Accordingly, any combination of codon optimization methods can be used. Exemplary methods include the high codon adaptation index (CAI) method, the Low U method, and others. The CAI method chooses a most frequently used synonymous codon for an entire protein coding sequence. As an example, the most frequently used codon for each amino acid can be deduced from 74,218 protein-coding genes from a human genome. The Low U method targets U-containing codons that can be replaced with a synonymous codon with fewer U moieties, generally without changing other codons. If there is more than one choice for replacement, the more frequently used codon can be selected. Any polynucleotide, nucleic acid sequence, or codon sequence provided herein can be codon-optimized. Expression vectors include all those known in the art, such as cosmids, plasmids (e.g., naked or contained in liposomes), retrotransposons (e.g. piggyback, sleeping beauty), and viruses (e.g., lentiviruses, retroviruses, adenoviruses, and adeno-associated viruses) that can incorporate and deliver the recombinant polynucleotide. Methods for producing viral vectors are known in the art. Typically, a disclosed virus is produced in a suitable host cell line using conventional techniques including culturing a transfected or infected host cell under suitable conditions so as to allow the production of infectious viral particles. Nucleic acids encoding viral genes and / or sequence(s) encoding two or more optimal HPV epitopes can be incorporated into plasmids and introduced into host cells through conventional transfection or Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT transformation techniques. Exemplary suitable host cells for production of disclosed viruses include human cell lines such as HeLa, Hela-S3, HEK293, 911, A549, HER96, or PER-C6 cells. Specific production and purification conditions will vary depending upon the virus and the production system employed. In some implementations, producer cells may be directly administered to a subject, however, in other implementations, following production, infectious viral particles are recovered from the culture and optionally purified. Typical purification steps may include plaque purification, centrifugation, e.g., cesium chloride gradient centrifugation, clarification, enzymatic treatment, e.g., benzonase or protease treatment, chromatographic steps, e.g., ion exchange chromatography or filtration steps. In certain implementations, the expression vector is a viral vector. The term "virus" is used herein to refer any of the obligate intracellular parasites having no protein-synthesizing or energy-generating mechanism. Exemplary viral vectors include retroviral vectors (e.g., lentiviral vectors), adenoviral vectors, adeno-associated viral vectors, herpesviruses vectors, Epstein-Barr virus (EBV) vectors, polyomavirus vectors (e.g., simian vacuolating virus 40 (SV40) vectors), poxvirus vectors, and pseudotype virus vectors. The virus may be an RNA virus (having a genome that is composed of RNA) or a DNA virus (having a genome composed of DNA). In certain implementations, the viral vector is a DNA virus vector. Exemplary DNA viruses include parvoviruses (e.g., adeno-associated viruses), adenoviruses, asfarviruses, herpesviruses (e.g., herpes simplex virus 1 and 2 (HSV-1 and HSV-2), Epstein-Barr virus (EBV), cytomegalovirus (CMV)), papillomoviruses (e.g., HPV), polyomaviruses (e.g., simian vacuolating virus 40 (SV40)), and poxviruses (e.g., vaccinia virus, cowpox virus, smallpox virus, fowlpox virus, sheeppox virus, myxoma virus). In certain implementations, the viral vector is a RNA virus vector. Exemplary RNA viruses include bunyaviruses (e.g., hantavirus), coronaviruses, ebolaviruses, flaviviruses (e.g., yellow fever virus, west nile virus, dengue virus), hepatitis viruses (e.g., hepatitis A virus, hepatitis C virus, hepatitis E virus), influenza viruses (e.g., influenza virus type A, influenza virus type B, influenza virus type C), measles virus, mumps virus, noroviruses (e.g., Norwalk virus), poliovirus, respiratory syncytial virus (RSV), retroviruses (e.g., human immunodeficiency virus- 1 (HIV-1)) and toroviruses. In certain implementations, the expression vector comprises a regulatory sequence or promoter operably linked to the nucleotide sequence encoding the two or more selected optimal HPV epitopes. The term "operably linked" refers to a linkage of polynucleotide elements in a functional relationship. A nucleic acid sequence is "operably linked" when it is placed into a functional relationship with another nucleic acid sequence. For instance, a promoter or enhancer is operably linked to a gene if it affects the transcription of the gene. Operably linked nucleotide sequences are typically contiguous. However, as enhancers generally function when separated from the promoter by several kilobases and intronic sequences may be of variable lengths, some polynucleotide elements may be operably linked but not directly flanked and may even function in trans from a different allele or chromosome. Nucleic acid sequences encoding two or more selected optimal HPV epitopes preferably have strong promoters that are active in a variety of cell types. The promoters for eukaryotic nucleic acid sequences are typically present within the structural sequences encoding the two or more optimal HPV epitopes itself. Although there are elements which regulate transcriptional activity within the 5' upstream region, the length of an active transcriptional unit may be considerably less than 500 base pairs. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Additional exemplary promoters which may be employed include, but are not limited to, the retroviral LTR, the SV40 promoter, the human cytomegalovirus (CMV) promoter, the U6 promoter, or any other promoter (e.g., cellular promoters such as eukaryotic cellular promoters including, but not limited to, the histone, RNA polymerase III (pol III), and β-actin promoters). Other viral promoters which may be employed include, but are not limited to, adenovirus promoters, thymidine kinase (TK) promoters, and B19 parvovirus promoters. The selection of a suitable promoter will be apparent to those skilled in the art from the teachings contained herein. In certain implementations, an expression vector is an adeno-associated virus (AAV) vector. AAV is a small, nonenveloped icosahedral virus of the genus Dependoparvovirus and family Parvovirus. AAV has a single-stranded linear DNA genome of approximately 4.7 kb. AAV is capable of infecting both dividing and quiescent cells of several tissue types, with different AAV serotypes exhibiting different tissue tropism. AAV includes numerous serologically distinguishable types including serotypes AAV- 1 to AAV- 12, as well as more than 100 serotypes from nonhuman primates (See, e.g., Srivastava (2008) J. Cell Biochem., 105(1): 17–24, and Gao et al. (2004) J. Virol., 78(12), 6381–6388). The serotype of the AAV vector used in the present invention can be selected by a skilled person in the art based on the efficiency of delivery, tissue tropism, and immunogenicity. For example, AAV-1, AAV-2, AAV-4, AAV-5, AAV-8, and AAV-9 can be used for delivery to the central nervous system; AAV-1, AAV-8, and AAV-9 can be used for delivery to the heart; AAV-2 can be used for delivery to the kidney; AAV-7, AAV-8, and AAV-9 can be used for delivery to the liver; AAV-4, AAV-5, AAV-6, AAV-9 can be used for delivery to the lung, AAV-8 can be used for delivery to the pancreas, AAV-2, AAV-5, and AAV-8 can be used for delivery to the photoreceptor cells; AAV-1, AAV-2, AAV-4, AAV-5, and AAV-8 can be used for delivery to the retinal pigment epithelium; AAV-1, AAV-6, AAV-7, AAV-8, and AAV-9 can be used for delivery to the skeletal muscle. In certain implementations, the AAV capsid protein comprises a sequence as disclosed in U.S. Patent No.7,198,951, such as, but not limited to, AAV-9 (SEQ ID NOs: 1-3 of U.S. Patent No.7,198,951), AAV-2 (SEQ ID NO: 4 of U.S. Patent No.7,198,951), AAV-1 (SEQ ID NO: 5 of U.S. Patent No. 7,198,951), AAV-3 (SEQ ID NO: 6 of U.S. Patent No.7,198,951), and AAV-8 (SEQ ID NO: 7 of U.S. Patent No.7,198,951). AAV serotypes identified from rhesus monkeys, e.g., rh.8, rh.10, rh.39, rh.43, and rh.74, are also contemplated in the instant invention. Besides the natural AAV serotypes, modified AAV capsids have been developed for improving efficiency of delivery, tissue tropism, and immunogenicity. Exemplary natural and modified AAV capsids are disclosed in U.S. Patent Nos.7,906,111, 9,493,788, and 7,198,951, and PCT Publication No. WO2017189964A2. The wild-type AAV genome contains two 145 nucleotide inverted terminal repeats (ITRs), which contain signal sequences directing AAV replication, genome encapsidation and integration. In addition to the ITRs, three AAV promoters, p5, p19, and p40, drive expression of two open reading frames encoding rep and cap genes. Two rep promoters, coupled with differential splicing of the single AAV intron, result in the production of four rep proteins (Rep 78, Rep 68, Rep 52, and Rep 40) from the rep gene. Rep proteins are responsible for genomic replication. The Cap gene is expressed from the p40 promoter, and encodes three capsid proteins (VP1, VP2, and VP3) which are splice variants of the cap gene. These proteins form the capsid of the AAV particle. Because the cis-acting signals for replication, encapsidation, and integration are contained within Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT the ITRs, some or all of the 4.3 kb internal genome may be replaced with foreign DNA, for example, an expression cassette for an exogenous nucleic acid sequence of interest encoding two or more optimal HPV epitopes. Accordingly, in certain implementations, the AAV vector comprises a genome comprising an expression cassette for an exogenous nucleic acid sequence encoding two or more optimal HPV epitopes flanked by a 5’ ITR and a 3’ ITR. The ITRs may be derived from the same serotype as the capsid or a derivative thereof. Alternatively, the ITRs may be of a different serotype from the capsid, thereby generating a pseudotyped AAV. In certain implementations, the ITRs are derived from AAV-2. In certain implementations, the ITRs are derived from AAV-5. At least one of the ITRs may be modified to mutate or delete the terminal resolution site, thereby allowing production of a self- complementary AAV vector. The rep and cap proteins can be provided in trans, for example, on a plasmid, to produce an AAV vector. A host cell line permissive of AAV replication must express the rep and cap genes, the ITR- flanked expression cassette, and helper functions provided by a helper virus, for example adenoviral genes E1a, E1b55K, E2a, E4orf6, and VA (Weitzman et al., Adeno-associated virus biology. Adeno- Associated Virus: Methods and Protocols, pp.1–23, 2011). Methods for generating and purifying AAV vectors have been described in detail (See e.g., Mueller et al., (2012) Current Protocols in Microbiology, 14D.1.1-14D.1.21, Production and Discovery of Novel Recombinant Adeno-Associated Viral Vectors). Numerous cell types are suitable for producing AAV vectors, including HEK293 cells, COS cells, HeLa cells, BHK cells, Vero cells, as well as insect cells (See e.g. U.S. Patent Nos.6,156,303, 5,387,484, 5,741,683, 5,691,176, 5,688,676, and 8,163,543, U.S. Patent Publication No.20020081721, and PCT Publication Nos. WO00 / 47757, WO00 / 24916, and WO96 / 17947). AAV vectors are typically produced in these cell types by one plasmid containing the ITR-flanked expression cassette, and one or more additional plasmids providing the additional AAV and helper virus genes. AAV of any serotype may be used in the present invention. Similarly, it is contemplated that any adenoviral type may be used, and a person of skill in the art will be able to identify AAV and adenoviral types suitable for the production of their desired recombinant AAV vector (rAAV). AAV particles may be purified, for example by affinity chromatography, iodixonal gradient, or cesium chloride (CsCl) gradient. AAV vectors may have single-stranded genomes that are 4.7 kb in size, or are larger or smaller than 4.7 kb, including oversized genomes that are as large as 5.2 kb, or as small as 3.0 kb. Thus, where the exogenous gene of interest to be expressed from the AAV vector is small, the AAV genome may comprise a stuffer sequence. Further, vector genomes may be substantially self-complementary thereby allowing for rapid expression in the cell. In certain implementations, the genome of a self-complementary AAV vector comprises from 5' to 3': a 5' ITR; a first nucleic acid sequence comprising a promoter and / or enhancer operably linked to a nucleic acid sequence encoding two or more optimal HPV epitopes; a modified ITR that does not have a functional terminal resolution site; a second nucleic acid sequence complementary or substantially complementary to the first nucleic acid sequence; and a 3' ITR. AAV vectors containing genomes of all types are suitable for use in the method of the present invention. Non-limiting examples of AAV vectors include pAAV-MCS (Agilent Technologies), pAAVK-EF1α- MCS (System Bio Catalog # AAV502A-1), pAAVK-EF1α-MCS1-CMV-MCS2 (System Bio Catalog # AAV503A-1), pAAV-ZsGreen1 (Clontech Catalog #6231), pAAV- MCS2 (Addgene Plasmid #46954), AAV-Stuffer (Addgene Plasmid #106248), pAAVscCBPIGpluc (Addgene Plasmid #35645), Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT AAVS1_Puro_PGK1_3xFLAG_Twin_Strep (Addgene Plasmid #68375), pAAV-RAM-d2TTA::TRE-MCS- WPRE-pA (Addgene Plasmid #63931), pAAV-UbC (Addgene Plasmid #62806), pAAVS1-P-MCS (Addgene Plasmid #80488), pAAV-Gateway (Addgene Plasmid #32671), pAAV-Puro_siKD (Addgene Plasmid #86695), pAAVS1-Nst-MCS (Addgene Plasmid #80487), pAAVS1-Nst-CAG-DEST (Addgene Plasmid #80489), pAAVS1-P-CAG-DEST (Addgene Plasmid #80490), pAAVf-EnhCB-lacZnls (Addgene Plasmid #35642), and pAAVS1-shRNA (Addgene Plasmid #82697). These vectors can be modified to be suitable for therapeutic use. For example, an exogenous nucleic acid sequence of interest encoding two or more selected optimal HPV epitopes can be inserted in a multiple cloning site, and a selection marker (e.g., puro or a gene encoding a fluorescent protein) can be deleted or replaced with another (same or different) exogenous gene of interest. Further examples of AAV vectors are disclosed in U.S. Patent Nos. 5,871,982, 6,270,996, 7,238,526, 6,943,019, 6,953,690, 9,150,882, and 8,298,818, U.S. Patent Publication No.2009 / 0087413, and PCT Publication Nos. WO2017075335A1, WO2017075338A2, and WO2017201258A1. In certain implementations, the viral vector can be a retroviral vector. Examples of retroviral vectors include Moloney murine leukemia virus vectors, spleen necrosis virus vectors, and vectors derived from retroviruses such as Rous sarcoma virus, Harvey sarcoma virus, avian leukosis virus, human immunodeficiency virus, myeloproliferative sarcoma virus, and mammary tumor virus. Retroviral vectors are useful as agents to mediate retroviral-mediated gene transfer into eukaryotic cells. In some implementations, the viral vector can be an adenoviral vector. Adenoviruses are medium-sized (90-100 nm), non-enveloped (naked), icosahedral viruses composed of a nucleocapsid and a double-stranded linear DNA genome. The term "adenovirus" refers to any virus in the genus Adenoviridiae including, but not limited to, human, bovine, ovine, equine, canine, porcine, murine, and simian adenovirus subgenera. Typically, an adenoviral vector is generated by introducing one or more mutations (e.g., a deletion, insertion, or substitution) into the adenoviral genome of the adenovirus so as to accommodate the insertion of a non-native nucleic acid sequence, for example, for gene transfer, into the adenovirus. A human adenovirus can be used as the source of the adenoviral genome for the adenoviral vector. For instance, an adenovirus can be of subgroup A (e.g., serotypes 12, 18, and 31), subgroup B (e.g., serotypes 3, 7, 11, 14, 16, 21, 34, 35, and 50), subgroup C (e.g., serotypes 1 , 2, 5, and 6), subgroup D (e.g., serotypes 8, 9, 10, 13, 15, 17, 19, 20, 22-30, 32, 33, 36-39, and 42-48), subgroup E (e.g., serotype 4), subgroup F (e.g., serotypes 40 and 41 ), an unclassified serogroup (e.g., serotypes 49 and 51), or any other adenoviral serogroup or serotype. In an exemplary implementation, the adenovirus vector is a serotype 5 adenovirus vector. Adenoviral serotypes 1 through 51 are available from the American Type Culture Collection (ATCC, Manassas, Virginia). Non-group C adenoviral vectors, methods of producing non-group C adenoviral vectors, and methods of using non- group C adenoviral vectors are disclosed in, for example, U.S. Patent Nos.5,801,030, 5,837,511, and 5,849,561, and PCT Publication Nos. WO1997 / 012986 and WO1998 / 053087. Non-human adenovirus (e.g., ape, simian, avian, canine, ovine, or bovine adenoviruses) can be used to generate the adenoviral vector (i.e., as a source of the adenoviral genome for the adenoviral vector). For example, the adenoviral vector can be based on a simian adenovirus, including both new Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT world and old world monkeys (see, e.g., Virus Taxonomy: VHIth Report of the International Committee on Taxonomy of Viruses (2005)). A phylogeny analysis of adenoviruses that infect primates is disclosed in, e.g., Roy et al. (2009) PLoS Pathog.5(7):e1000503. A gorilla adenovirus can be used as the source of the adenoviral genome for the adenoviral vector. Gorilla adenoviruses and adenoviral vectors are described in, e.g., PCT Publication Nos. WO2022 / 003083, WO2013 / 052799, WO2013 / 052811, and WO2013 / 052832, the contents each of which are expressly incorporated herein by reference. The adenoviral vector can also comprise a combination of subtypes and thereby be a "chimeric" adenoviral vector. The adenoviral vector can be replication-competent, conditionally replication- competent, or replication-deficient. A replication-competent adenoviral vector can replicate in typical host cells, i.e., cells typically capable of being infected by an adenovirus. A conditionally-replicating adenoviral vector is an adenoviral vector that has been engineered to replicate under pre-determined conditions. For example, replication-essential gene functions, e.g., gene functions encoded by the adenoviral early regions, can be operably linked to an inducible, repressible, or tissue-specific transcription control sequence, e.g., a promoter. Conditionally-replicating adenoviral vectors are further described in U.S. Patent No.5,998,205. A replication-deficient adenoviral vector is an adenoviral vector that requires complementation of one or more gene functions or regions of the adenoviral genome that are required for replication, as a result of, for example, a deficiency in one or more replication- essential gene function or regions, such that the adenoviral vector does not replicate in typical host cells, especially those in a human to be infected by the adenoviral vector. The adenoviral vector can be replication-deficient, such that the replication- deficient adenoviral vector requires complementation of at least one replication-essential gene function of one or more regions of the adenoviral genome for propagation (e.g., to form adenoviral vector particles). The adenoviral vector can be deficient in one or more replication-essential gene functions of only the early regions (i.e., E1-E4 regions) of the adenoviral genome, only the late regions (i.e., L1-L5 regions) of the adenoviral genome, both the early and late regions of the adenoviral genome, or all adenoviral genes (i.e., a high capacity adenovector (HC-Ad)). See, e.g., Morsy et al. (1998) Proc. Natl. Acad. Sci. USA 95: 965-976, Chen et al. (1997) Proc. Natl. Acad. Sci. USA 94: 1645-1650, and Kochanek et al. (1999) Hum. Gene Ther.10(15):2451-9. Examples of replication-deficient adenoviral vectors are disclosed in U.S. Patent Nos.5,837,511, 5,851,806, 5,994,106, 6,127,175, 6,482,616, and 7,195,896, and PCT Publication Nos. WO1994 / 028152, WO1995 / 002697, WO1995 / 016772, WO1995 / 034671, WO1996 / 022378, WO1997 / 012986, WO1997 / 021826, and WO2003 / 022311. The replication-deficient adenoviral vector of the invention can be produced in complementing cell lines that provide gene functions not present in the replication-deficient adenoviral vector, but required for viral propagation, at appropriate levels in order to generate high titers of viral vector stock. Such complementing cell lines are known and include, but are not limited to, 293 cells (described in, e.g., Graham et al. (1977) J. Gen. Virol.36: 59-72), PER.C6 cells (described in, e.g., PCT Publication No. WO1997 / 000326, and U.S. Patent Nos.5,994,128 and 6,033,908), and 293-ORF6 cells (described in, e.g., PCT Publication No. WO1995 / 034671 and Brough et al. (1997) J. Virol.71: 9206-9213). Other suitable complementing cell lines to produce the replication-deficient adenoviral vector of the invention include complementing cells that have been generated to propagate adenoviral vectors encoding Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT transgenes whose expression inhibits viral growth in host cells (see, e.g., U.S. Patent Publication No. 2008 / 0233650). Additional suitable complementing cells are described in, for example, U.S. Patent Nos. 6,677,156 and 6,682,929, and PCT Publication No. WO2003 / 020879. Formulations for adenoviral vector- containing compositions are further described in, for example, U.S. Patent Nos.6,225,289, and 6,514,943, and PCT Publication No. WO2000 / 034444. Additional exemplary adenoviral vectors, and / or methods for making or propagating adenoviral vectors are described in U.S. Patent Nos.5,559,099, 5,837,511, 5,846,782, 5,851,806, 5,994,106, 5,994,128, 5,965,541, 5,981,225, 6,040,174, 6,020,191, 6,083,716, 6,113,913, 6,303,362, 7,067,310, and 9,073,980. Commercially available adenoviral vector systems include the ViraPower™ Adenoviral Expression System available from Thermo Fisher Scientific, the AdEasy™ adenoviral vector system available from Agilent Technologies, and the Adeno-X™ Expression System 3 available from Takara Bio USA, Inc. In certain implementations, the viral vector can be a Herpes Simplex Virus plasmid vector. Herpes simplex virus type-l (HSV-1) has been demonstrated as a potential useful gene delivery vector system for gene therapy. HSV-1 vectors have been used for transfer of genes to muscle, and have been used for murine brain tumor treatment. Helper virus dependent mini-viral vectors have been developed for easier operation and their capacity for larger insertion (up to 140 kb). Replication incompetent HSV amplicons have been constructed in the art. These HSV amplicons contain large deletions of the HSV genome to provide space for insertion of exogenous DNA. Typically, they comprise the HSV-1 packaging site, the HSV-1 "ori S" replication site and the IE 4 / 5 promoter sequence. These virions are dependent on a helper virus for propagation. In some implementations, the recombinant vector is a Vaccinia vector. Vaccinia are recombinant vaccines typically are used as vectors for expression of foreign genes within a host, in order to generate an in vivo immune response. In certain implementations, a Vaccinia vector for use in an immunogen composition described herein is a highly attenuated strain of a Vaccinia virus, such as Modified Vaccinia Ankara (MVA) virus. MVA can encode more than one foreign antigen and thus can effectively function as a multivalent vaccine. In animal models, MVA vector vaccines have been found to have intrinsic adjuvant capacities and be immunogenic and protective against various infectious agents including immunodeficiency viruses. Compared to replicating Vaccinia viruses, MVA provides similar or higher levels of recombinant gene expression even in non-permissive cells. In some implementations, the recombinant vector can include messenger RNA (mRNA). One advantage of mRNA is that mRNA vaccines are capable of inducing a balanced immune response including both cellular and humoral immunity. In addition, mRNA vaccines can be designed to be self- adjuvanting. Alternatively, mRNA vaccines can be supplemented with one or more additional adjuvant molecules such as additional mRNAs encoding auxiliary adjuvant molecules. Functional synthetic mRNA may be obtained by in vitro transcription of a cDNA template, typically plasmid DNA (pDNA), using a bacteriophage RNA polymerase. Synthetic mRNA for use in an mRNA vector immunogen composition described herein can include a protein-encoding open reading frame (ORF) flanked at the minimum by two elements essential for the function of mature eukaryotic mRNA: a “cap,” i.e., a 7-methyl-guanosine residue joined to the 5′-end via a 5′-5′ triphosphate, and a poly(A) tail at Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT the 3′-end. Therefore, in some implementations, a pDNA template can include a bacteriophage promoter, an ORF, optionally a poly(d(A / T)) sequence transcribed into poly(A) and a unique restriction site for linearization of the plasmid to ensure defined termination of transcription. A linearized pDNA template can be transcribed into mRNA in a mixture including recombinant RNA polymerase (T7, T3 or SP6) and nucleoside triphosphates. To obtain capped mRNA by transcription a cap analog like the dinucleotide m7G(5′)-ppp-(5′)G may be included in the reaction. If the cap analog is in excess of GTP, transcription initiates with the cap analog rather than GTP, yielding capped mRNA. Alternatively, the cap may be added enzymatically post transcription. A poly(A) tail may also be added post transcription if it is not provided by the pDNA template. Following transcription, the pDNA template as well as contaminating bacterial DNA is digested by DNase. The resultant mRNA transcript can be purified by a combination of precipitation and extraction steps. In order to be translated and elicit an antigen-specific immune response, an mRNA- vaccine has to reach the cytosol of target cells. However, as opposed to DNA vaccines, RNA vaccines only have to cross the plasma membrane, but not the nuclear envelope which may improve the probability of successful in vivo transfection. While locally administered naked mRNA can be taken up by cells, the efficacy of mRNA vaccines may benefit significantly from complexing agents which protect RNA from degradation. Complexing agents can be tailored to the specific route of delivery. Complexation may also enhance uptake by cells and / or improve delivery to the translation machinery in the cytoplasm. Thus, in some implementations, mRNA for use in an immunogen composition can be complexed with either lipids or polymers. In some implementations, the vector is a delivery vehicle comprised of lipid-based compositions, including lipid nanoparticle compositions include but are not limited those described in U.S. Patent Publication Number 20200206362, filed as U.S. Patent Application Serial number 16 / 599661 on October 11, 2019 and U.S. Patent Number 10,799,463, the contents of which are incorporated herein by reference. In some embodiments of the present disclosure, an RNA molecule is "replicon RNA" or “replicon RNA molecule” or simply a "replicon", in particular "self-replicating RNA" or "self- amplifying RNA" or “replicable RNA molecule”. A replicon RNA molecule is an RNA that is able to be replicated by an RNA- dependent RNA polymerase (replicase) by virtue of comprising nucleotide sequences that can be recognized by the replicase such that the RNA is replicated. The replicon does not necessarily encode the replicase, such that replicons can be replicated in cis (by the encoded replicase; also called a “cis- replicon”) or in trans (by a replicase provided in another manner, e.g., a separate replicase encoding nucleic acid, such as an mRNA; also called “trans-replicon”). In self-amplifying (saRNA) vaccine constructs, the ORF encoding viral structural proteins is replaced with any antigen of choice, while the viral replicase remains an integral part of the vaccine and drives intracellular amplification of the RNA after immunization. Therefore, in some embodiments, the recombinant vector can include a saRNA vaccine construct where the ORF encoding viral structural proteins have been replaced with immunogens of the invention. In certain embodiments, the replicon or self-replicating RNA is derived from or comprises elements derived from a single stranded RNA (ssRNA) virus, in particular a positive-stranded ssRNA Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT virus such as an alphavirus. Alphaviruses are typical representatives of positive-stranded RNA viruses. Alphaviruses replicate in the cytoplasm of infected cells (for review of the alphaviral life cycle see José et al., Future Microbiol., 2009, vol.4, pp.837–856). The total genome length of many alphaviruses typically ranges between 11,000 and 12,000 nucleotides, and the genomic RNA typically has a 5’-cap, and a 3’ poly(A) tail. The genome of alphaviruses encodes non-structural proteins (involved in transcription, modification and replication of viral RNA and in protein modification) and structural proteins (forming the virus particle). There are typically two open reading frames (ORFs) in the genome. The four non-structural proteins (nsP1–nsP4) are typically encoded together by a first ORF beginning near the 5′ terminus of the genome, while alphavirus structural proteins are encoded together by a second ORF which is found downstream of the first ORF and extends near the 3’ terminus of the genome. Typically, the first ORF is larger than the second ORF, the ratio being roughly 2:1. In cells infected by an alphavirus, only the nucleic acid sequence encoding non-structural proteins is translated from the genomic RNA, while the genetic information encoding structural proteins is translatable from a subgenomic transcript, which is an RNA molecule that resembles eukaryotic messenger RNA (mRNA; Gould et al., 2010, Antiviral Res., vol.87 pp.111–124). Following infection, i.e. at early stages of the viral life cycle, the (+) stranded genomic RNA directly acts like a messenger RNA for the translation of the open reading frame encoding the non- structural poly-protein (nsP1234). Alphavirus-derived vectors have been proposed for delivery of foreign genetic information into target cells or target organisms. In simple approaches, the open reading frame encoding alphaviral structural proteins is replaced by an open reading frame encoding a protein of interest. Alphavirus-based trans-replication systems rely on alphavirus nucleotide sequence elements on two separate nucleic acid molecules: one nucleic acid molecule encodes a viral replicase, and the other nucleic acid molecule is capable of being replicated by said replicase in trans (hence the designation trans-replication system). Trans-replication requires the presence of both these nucleic acid molecules in a given host cell. The nucleic acid molecule capable of being replicated by the replicase in trans must comprise certain alphaviral sequence elements to allow recognition and RNA synthesis by the alphaviral replicase. Nucleic acids can be administered with one or more delivery vehicles that protect the nucleic acids from degradation, maximize delivery to on-target cells and minimize exposure to off-target cells. Such nucleic acid delivery vehicles may complex or encapsulate nucleic acids and include a range of materials, including polymers and lipids. In some embodiments, such nucleic acid delivery vehicles may form particles with nucleic acids, preferably RNA. RNA, in particular mRNA, described herein may be present in particles comprising (i) the RNA, and (ii) at least one cationic or cationically ionizable compound such as a polymer or lipid complexing the RNA. Electrostatic interactions between positively charged molecules such as polymers and lipids and negatively charged RNA are involved in particle formation. This results in complexation and spontaneous formation of nucleic acid, in particular RNA, particles. Different types of nucleic acid containing particles have been described previously to be suitable for delivery of RNA in particulate form (cf., e.g., Kaczmarek, J. C. et al., 2017, Genome Medicine 9, 60). For non-viral RNA delivery vehicles, nanoparticle encapsulation of nucleic acids physically protects the nucleic acids from degradation and, depending on the specific chemistry, can aid in cellular uptake and Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT endosomal escape. In the context of the present disclosure, the term "particle" relates to a structured entity formed by molecules or molecule complexes, in particular particle forming compounds. In some embodiments, the particle contains an envelope (e.g., one or more layers or lamellas) made of one or more types of amphiphilic substances (e.g., amphiphilic lipids). In this context, the expression "amphiphilic substance" means that the substance possesses both hydrophilic and lipophilic properties. The envelope may also comprise additional substances (e.g., additional lipids) which do not have to be amphiphilic. Thus, the particle may be a monolamellar or multilamellar structure, wherein the substances constituting the one or more layers or lamellas comprise one or more types of amphiphilic substances (in particular selected from the group consisting of amphiphilic lipids) optionally in combination with additional substances (e.g., additional lipids) which do not have to be amphiphilic. In some embodiments, the term "particle" relates to a micro- or nano-sized structure, such as a micro- or nano-sized compact structure. According to the present disclosure, the term "particle" includes nanoparticles. A "DNA particle", "RNA particle" or "DNA and RNA particle" can be used to deliver DNA and / or RNA to a target site of interest (e.g., cell, tissue, organ, and the like). A DNA and / or RNA particle may be formed from lipids comprising at least one cationic or cationically ionizable lipid. Without intending to be bound by any theory, it is believed that the cationic or cationically ionizable lipid combines together with the nucleic acids to form aggregates, and this aggregation results in colloidally stable particles. RNA particles described herein include lipid nanoparticle (LNP)-based and lipoplex (LPX)-based formulations. A lipoplex (LPX) described herein is obtainable from mixing two aqueous phases, namely a phase comprising RNA and a phase comprising a dispersion of lipids. In some embodiments, the lipid phase comprises liposomes. In some embodiments, liposomes are self-closed unilamellar or multilamellar vesicular particles wherein the lamellae comprise lipid bilayers and the encapsulated lumen comprises an aqueous phase. A prerequisite for using liposomes for nanoparticle formation is that the lipids in the mixture as required are able to form lamellar (bilayer) phases in the applied aqueous environment. In some embodiments, liposomes comprise unilamellar or multilamellar phospholipid bilayers enclosing an aqueous core (also referred to herein as an aqueous lumen). They may be prepared from materials possessing polar head (hydrophilic) groups and nonpolar tail (hydrophobic) groups. In some embodiments, cationic lipids employed in formulating liposomes designed for the delivery of RNA are amphiphilic in nature and consist of a positively charged (cationic) amine head group linked to a hydrocarbon chain or cholesterol derivative via glycerol. In some embodiments, lipoplexes are multilamellar liposome-based formulations that form upon electrostatic interaction of cationic liposomes with nucleic acids. In some embodiments, formed lipoplexes possess distinct internal arrangements of molecules that arise due to the transformation from liposomal structure into compact RNA–lipoplexes. In some embodiments, an LPX particle comprises an amphiphilic lipid, in particular cationic or cationically ionizable amphiphilic lipid, and RNA (especially mRNA) as described herein. In some embodiments, electrostatic interactions between positively charged liposomes (made from one or more amphiphilic lipids, in particular cationic or cationically ionizable amphiphilic lipids) and negatively charged RNA (especially mRNA) results in complexation and spontaneous formation of RNA lipoplex particles. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Positively charged liposomes may be generally synthesized using a cationic or cationically ionizable amphiphilic lipid, such as 1,2-di-O-octadecenyl-3-trimethylammonium propane (DOTMA) and / or 1,2- dioleyloxy-3-dimethylaminopropane (DODMA), and optionally additional lipids, such as dioleoylphosphatidylethanolamine (DOPE) or distearoylphosphatidylcholine (DSPC). In general, a lipid nanoparticle (LNP) is typically obtainable from direct mixing of RNA in an aqueous phase with lipids in a phase comprising an organic solvent, such as ethanol. In that case, lipids or lipid mixtures can be used for particle formation, which do not form lamellar (bilayer) phases in water. In some embodiments, LNPs comprise or consist of a cationic / cationically ionizable lipid and helper lipids such as phospholipids, cholesterol, and / or polymer-conjugated lipids (e.g., polyethylene glycol (PEG) lipids). In some embodiments, in the RNA LNPs described herein the RNA (in particular, mRNA) is bound by cationically ionizable lipid that occupies the central core of the LNP. In some embodiments, polymer-conjugated lipid forms the surface of the LNP, along with phospholipids. In some embodiments, cholesterol and cationically ionizable lipid in charged and uncharged forms can be distributed throughout the LNP. In some embodiments, RNA (e.g., mRNA) described herein may be noncovalently associated with a particle as described herein. In embodiments, the RNA (especially mRNA) may be adhered to the outer surface of the particle (surface RNA (especially surface mRNA)) and / or may be contained in the particle (encapsulated RNA (especially encapsulated mRNA)). Given their high degree of chemical flexibility, polymers are commonly used materials for nanoparticle-based delivery. Typically, cationic polymers are used to electrostatically condense the negatively charged RNA into particles, in particular nanoparticles. These positively charged groups often consist of amines that change their state of protonation in the pH range between 5.5 and 7.5, thought to lead to an ion imbalance that results in endosomal rupture. Polymers such as poly-L-lysine, polyamidoamine, protamine and polyethyleneimine, as well as naturally occurring polymers such as chitosan have all been applied to nucleic acid delivery and are suitable as cationic polymers herein. In addition, some investigators have synthesized polymers specifically for nucleic acid delivery. Poly(β- amino esters), in particular, have gained widespread use in nucleic acid delivery owing to their ease of synthesis and biodegradability. Such synthetic polymers are also suitable as cationic polymers herein. A "polymer," as used herein, is given its ordinary meaning, i.e., a molecular structure comprising one or more repeat units (monomers), connected by covalent bonds. The repeat units can all be identical, or in some cases, there can be more than one type of repeat unit present within the polymer. In some cases, the polymer is biologically derived, i.e., a biopolymer such as a protein. In some cases, additional moieties can also be present in the polymer, for example targeting moieties. If more than one type of repeat unit is present within the polymer, then the polymer is said to be a "copolymer." It is to be understood that the polymer being employed herein can be a copolymer. The repeat units forming the copolymer can be arranged in any fashion. For example, the repeat units can be arranged in a random order, in an alternating order, or as a "block" copolymer, i.e., comprising one or more regions each comprising a first repeat unit (e.g., a first block), and one or more regions each comprising a second repeat unit (e.g., a second block), etc. Block copolymers can have two (a diblock copolymer), three (a triblock copolymer), or more numbers of distinct blocks. In certain embodiments, the polymer is biocompatible. Biocompatible polymers are polymers that Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT typically do not result in significant cell death at moderate concentrations. In certain embodiments, the biocompatible polymer is biodegradable, i.e., the polymer is able to degrade, chemically and / or biologically, within a physiological environment, such as within the body. In certain embodiments, polymer may be protamine or polyalkyleneimine. The term "protamine" refers to any of various strongly basic proteins of relatively low molecular weight that are rich in arginine and are found associated especially with DNA in place of somatic histones in the sperm cells of various animals (as fish). In particular, the term "protamine" refers to proteins found in fish sperm that are strongly basic, are soluble in water, are not coagulated by heat, and yield chiefly arginine upon hydrolysis. In purified form, they are used in a long-acting formulation of insulin and to neutralize the anticoagulant effects of heparin. According to the disclosure, the term "protamine" as used herein is meant to comprise any protamine amino acid sequence obtained or derived from natural or biological sources including fragments thereof and multimeric forms of said amino acid sequence or fragment thereof as well as (synthesized) polypeptides which are artificial and specifically designed for specific purposes and cannot be isolated from native or biological sources. In one embodiment, the polyalkyleneimine comprises polyethylenimine and / or polypropylenimine, preferably polyethyleneimine. A preferred polyalkyleneimine is polyethyleneimine (PEI). The average molecular weight of PEI is preferably 0.75∙102 to 107 Da, preferably 1000 to 105 Da, more preferably 10000 to 40000 Da, more preferably 15000 to 30000 Da, even more preferably 20000 to 25000 Da. Cationic polymers (including polycationic polymers) contemplated for use herein include any cationic polymers which are able to electrostatically bind nucleic acid. In one embodiment, cationic polymers contemplated for use herein include any cationic polymers with which nucleic acid can be associated, e.g. by forming complexes with the nucleic acid or forming vesicles in which the nucleic acid is enclosed or encapsulated. Particles described herein may also comprise polymers other than cationic polymers, i.e., non- cationic polymers and / or anionic polymers. Collectively, anionic and neutral polymers are referred to herein as non-cationic polymers. As an alternative to direct injection of mRNA, an immune response may also be induced by vaccination with antigen-presenting cells (APCs) transfected with mRNA ex vivo where the APCs (e.g., dendritic cells (DCs)) are infused into the subject in need thereof. Transfection of DCs with mRNA encoding two or more optimal HPV epitopes can be accomplished with the use of a cationic lipid, i.e., DOTAP, or electroporation. Typically, approaches for DC-based vaccination are mainly based on antigen loading on in vitro- generated DCs from monocytes or CD34+cells, activating them with different toll-like receptor (TLR) ligands, cytokine combinations, and injecting them back to a subject in need thereof. DCs can be loaded through incubation with peptides (such as peptide-based vaccine compositions described below), proteins, RNA, or autologous / allogeneic tumor cells. Peptides can loaded directly on the MHC molecules on the surface of the DCs. In addition to RNA electroporation, antigens can be loaded into DCs using bacterial or viral vector transduction. Peptides or proteins can be loaded into DCs and provided one or more maturation stimuli such as proinflammaroty cytokines, CD40 Ligand (CD40L), and / or TLR agonists. In some implementations, bacterial or viral vectors can be used to target DCs with antigens. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Exemplary vectors used to target DCs can include, but are not limited to, vectors derived from bacteria such as bacillus Calmette-Guerin (BCG), Listeria monocytogenes, Salmonella, and Shigella, and viruses including Canarypox virus, Newcastle disease virus, vaccinia virus, Sindbis virus, yellow fever virus, human papillomavirus, adenovirus, adeno-associated virus, and lentiviruses. In certain implementations, the number of antigen loaded DCs administered to a subject can range from about 0.3 × 106cells to about 200 × 106cells per administration. A typical DC vaccination schedule can range from once every 2 weeks vs 3-4 doses or even up to 10 doses given every 3-4 weeks). The route of antigen loaded DC administration to a subject in need thereof can include injection, for example, subcutaneous, intradermal, intranodal, intravenous, or even intratumoral injection. In some implementations, administration strategies include administration of DC vaccines via more than one route, i.e., intradermally plus intravenously to induce a systemic response, and / or administration directly into the lymph nodes (intranodally). In some implementations, a T cell immunogen composition can include a peptide-based vaccine. For example, two or more selected optimal HPV epitope recombinant peptides for vaccination can be produced by expressing the immunogenic peptides in a heterologous expression system, e.g., a yeast expression system. Once purified, recombinant immunogenic peptides are typically administered to a subject with an adjuvant to boost the immune response. Delivery systems used for peptide vaccine use are typically able to protect protease- sensitive epitopes from degradation, and also allow for co-deliver of additional vaccine components such as an adjuvant. Exemplary peptide vaccine delivery systems can include, but are not limited to polymers, lipids (including liposomes, exosomes), inorganic particles, microparticles, nanoparticles, and carbon nanotubes. As described in more detail below, the T cell immunogen composition can be used to form a therapeutic composition, such as a vaccine or pharmaceutical composition. While it is possible that a vaccine can comprise the T cell immunogen composition in a pure or substantially pure form, it will be appreciated that the vaccine can additionally or optionally include the T cell immunogen composition and a pharmaceutically acceptable carrier or other therapeutic agent. For example, the pharmaceutically acceptable carrier can include a physiologically acceptable diluent, such as sterile water or sterile isotonic saline. As used herein, the term “pharmaceutically acceptable carrier” can refer to any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like. Additional components that may be present with the T cell immunogen composition can include adjuvants, preservatives, chemical stabilizers, and / or other proteins. It will be appreciated that the T cell immunogen composition can be conjugated with one or more lipoproteins, administered in liposomal form, or with an adjuvant. For example, to be efficient, vaccines can include a strong adjuvant supplying a signal for the initiation and support of the adaptive immune response in addition to an appropriate antigen, e.g., two or more selected optimal HPV epitopes. Typically, stabilizers, adjuvants, and preservatives are optimized to determine the best formulation for efficacy in a subject. Exemplary preservatives can include, but are not limited to, chiorobutanol, potassium sorbate, sorbic acid, sulfur dioxide, propyl gallate, the parabens, ethyl vanillin, glycerin, phenol, and parachiorophenol. Suitable stabilizing ingredients can include, for example, casamino acids, sucrose, gelatin, phenol red, N-Z amine, monopotassium diphosphate, lactose, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT lactalbumin hydrolysate, and dried milk. Other examples of pharmaceutically acceptable carriers are known in the art and described below. A T cell immunogen composition described herein administered to a subject as an HPV vaccine can be used either prophylactically or therapeutically. When provided prophylactically, the vaccine can be provided in advance of any evidence of an active HPV infection and thereby attenuate or prevent HPV infection. For example, a human subject at high risk for HPV infection can be prophylactically treated with a vaccine comprising the T cell immunogen composition and a pharmaceutically acceptable carrier. When provided therapeutically, the vaccine can be used to induced new T cell responses or enhance a subject’s own immune response to the antigens present as a result of HPV infection or HPV-associated malignancy. Thus, in some implementations, a therapeutically and / or prophylactically effective amount of T cell immunogen composition described herein is an amount that elicits an immune response to two or more optimal HPV epitopes and thereby prevents or inhibits HPV infection or clears HPV-associated malignancy in the subject. Inhibiting a viral infection can refer to inhibiting the onset of a viral infection, inhibiting an increase in an existing viral infection, or reducing the severity of or clearing the viral infection and / or malignancy. In this regard, one of ordinary skill in the art will appreciate that while complete inhibition of the onset of a viral infection is desirable, any degree of inhibition of the onset of a viral infection or clearance of viral- associated malignancy is beneficial. Likewise, one of ordinary skill in the art will appreciate that while elimination of viral infection is desirable, any degree of inhibition of an increase in an existing viral infection, progression of viral-associated malignancy or any degree of a reduction of a viral infection or is beneficial. Inhibition of a viral infection can be assayed by methods known in the art, such as by assessing viral load. Viral loads can be measured by methods known in the art, such as by using PCR to detect the presence of viral nucleic acids or antibody-based assays to detect the presence of viral protein in a sample (e.g., blood) from a subject. Assessment of viral-associated malignancy can be determined by methods known in the art, such as tissue biopsy and radiologic imaging of human subjects. Tissue biopsies can be measured by methods known on the art, such as antibody-based immunohistochemistry to detect viral antigen and PCR to detect the viral nucleic acids. Radiologic imaging can be used on human subjects to assess size and radiographic features of a viral-associated malignancy. Optimal dosages to be administered may be readily determined by those skilled in the art, and will vary with the particular compound used, the strength of the preparation, the mode of administration, and the advancement of the disease condition. In addition, factors associated with the particular patient being treated, including patient age, weight, diet and time of administration, will result in the need to adjust dosages. As noted above, compositions described herein may be combined with one or more additional therapeutic agents useful in the treatment of HPV infection. It will be understood that the scope of combinations of the compounds of this invention with HPV antivirals, immunomodulators, anti-infectives or vaccines is not limited to the following list and includes in principle any combination with any pharmaceutical composition useful for the treatment of HPV infection. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT The additional therapeutic agent may be used individually, sequentially, or in combination with one or more other such therapeutic agents described herein (e.g., HPV antivirals). Administration to a subject may be by the same or different route of administration or together in the same pharmaceutical formulation. Coadministration in the context of this invention is defined to mean the administration of more than one therapeutic agent in the course of a coordinated treatment to achieve an improved clinical outcome. Such coadministration may also be coextensive, that is, occurring during overlapping periods of time. Pharmaceutical compositions described herein can be formulated by standard techniques using one or more physiologically acceptable carriers or excipients. Suitable pharmaceutical carriers are described herein and in “Remington's Pharmaceutical Sciences” by E. W. Martin. The small molecule compounds of the present invention and their physiologically acceptable salts and solvates can be formulated for administration by any suitable route, including via inhalation, topically, nasally, orally, parenterally, or rectally. Thus, the administration of the pharmaceutical composition may be made by intradermal, subdermal, intravenous, intramuscular, intranasal, intracerebral, intratracheal, intraarterial, intraperitoneal, intravesical, intrapleural, intracoronary or intratumoral injection, with a syringe or other devices. Transdermal administration is also contemplated, as are inhalation or aerosol administration. Tablets and capsules can be administered orally, rectally or vaginally. For oral administration, a pharmaceutical composition or a medicament can take the form of, for example, a tablets or a capsule prepared by conventional means with a pharmaceutically acceptable excipient. Preferred are tablets and gelatin capsules comprising the active ingredient, i.e., a small molecule compound of the present invention, together with (a) diluents or fillers, e.g., lactose, dextrose, sucrose, mannitol, sorbitol, cellulose (e.g., ethyl cellulose, microcrystalline cellulose), glycine, pectin, polyacrylates and / or calcium hydrogen phosphate, calcium sulfate; (b) lubricants, e.g., silica, talcum, stearic acid, its magnesium or calcium salt, metallic stearates, colloidal silicon dioxide, hydrogenated vegetable oil, corn starch, sodium benzoate, sodium acetate and / or polyethyleneglycol; for tablets also (c) binders, e.g., magnesium aluminum silicate, starch paste, gelatin, tragacanth, methylcellulose, sodium carboxymethylcellulose, polyvinylpyrrolidone and / or hydroxypropyl methylcellulose; if desired (d) disintegrants, e.g., starches (e.g., potato starch or sodium starch), glycolate, agar, alginic acid or its sodium salt, or effervescent mixtures; (e) wetting agents, e.g., sodium lauryl sulphate, and / or (f) absorbents, colorants, flavors and sweeteners. Tablets may be either film coated or enteric coated according to methods known in the art. Liquid preparations for oral administration can take the form of, for example, solutions, syrups, or suspensions, or they can be presented as a dry product for constitution with water or other suitable vehicle before use. Such liquid preparations can be prepared by conventional means with pharmaceutically acceptable additives, for example, suspending agents, for example, sorbitol syrup, cellulose derivatives, or hydrogenated edible fats; emulsifying agents, for example, lecithin or acacia; non-aqueous vehicles, for example, almond oil, oily esters, ethyl alcohol, or fractionated vegetable oils; and preservatives, for example, methyl or propyl-p-hydroxybenzoates or sorbic acid. The preparations can also contain buffer salts, flavoring, coloring, and / or sweetening agents as appropriate. If desired, preparations for oral administration can be suitably formulated to give controlled release of the active compound. Pharmaceutical compositions described herein can be formulated for parenteral administration by Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT injection, for example by bolus injection or continuous infusion. Formulations for injection can be presented in unit dosage form, for example, in ampoules or in multi-dose containers, with an added preservative. Injectable compositions are preferably aqueous isotonic solutions or suspensions, and suppositories are preferably prepared from fatty emulsions or suspensions. The compositions may be sterilized and / or contain adjuvants, such as preserving, stabilizing, wetting or emulsifying agents, solution promoters, salts for regulating the osmotic pressure and / or buffers. Alternatively, the active ingredient can be in powder form for constitution with a suitable vehicle, for example, sterile pyrogen-free water, before use. In addition, they may also contain other therapeutically valuable substances. The compositions are prepared according to conventional mixing, granulating or coating methods, respectively, and contain about 0.1 to 75%, preferably about 1 to 50%, of the active ingredient. For administration by inhalation, the compounds may be conveniently delivered in the form of an aerosol spray presentation from pressurized packs or a nebulizer, with the use of a suitable propellant, for example, dichlorodifluoromethane, trichlorofluoromethane, dichlorotetrafluoroethane, carbon dioxide, or other suitable gas. In the case of a pressurized aerosol, the dosage unit can be determined by providing a valve to deliver a metered amount. Capsules and cartridges of, for example, gelatin for use in an inhaler or insufflator can be formulated containing a powder mix of the compound and a suitable powder base, for example, lactose or starch. Suitable formulations for transdermal application include an effective amount of a compound of the present invention with carrier. Preferred carriers include absorbable pharmacologically acceptable solvents to assist passage through the skin of the host. For example, transdermal devices are in the form of a bandage comprising a backing member, a reservoir containing the compound optionally with carriers, optionally a rate controlling barrier to deliver the compound to the skin of the host at a controlled and predetermined rate over a prolonged period of time, and means to secure the device to the skin. Matrix transdermal formulations may also be used. Suitable formulations for topical application, e.g., to the skin and eyes, are preferably aqueous solutions, ointments, creams or gels well-known in the art. Such may contain solubilizers, stabilizers, tonicity enhancing agents, buffers and preservatives. A pharmaceutical composition for use in a method described herein can also be formulated in rectal compositions, for example, suppositories or retention enemas, for example, containing conventional suppository bases, for example, cocoa butter or other glycerides. Furthermore, the pharmaceutical compositions can be formulated as a depot preparation. Such long-acting formulations can be administered by implantation (for example, subcutaneously or intramuscularly) or by intramuscular injection. Thus, for example, the compounds can be formulated with suitable polymeric or hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, or as sparingly soluble derivatives, for example, as a sparingly soluble salt. The compositions can, if desired, be presented in a pack or dispenser device that can contain one or more unit dosage forms containing the active ingredient. The pack can, for example, comprise metal or plastic foil, for example, a blister pack. The pack or dispenser device can be accompanied by instructions for administration. In one implementation, a pharmaceutical composition is administered to a subject, preferably a human, at a therapeutically effective dose to prevent, treat, or control a condition or disease as described Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT herein, such as HPV-associated infection or malignancy. The dosage of pharmaceutical compositions administered is dependent on the species of warm- blooded animal (mammal), the body weight, age, individual condition, surface area of the area to be treated and on the form of administration. The size of the dose also will be determined by the existence, nature, and extent of any adverse effects that accompany the administration of a particular small molecule compound in a particular subject. Typically, a dosage of the active compounds of the present invention is a dosage that is sufficient to achieve the desired effect. Optimal dosing schedules can be calculated from measurements of compound accumulation in the body of a subject. In general, dosage may be given once or more weekly, or monthly. Persons of ordinary skill in the art can easily determine optimum dosages, dosing methodologies and repetition rates. In another implementation, a pharmaceutical composition including a T cell immunogen composition described herein is administered in a daily dose in the range from about µg per kg of subject weight (0.1 µg / kg) to about 1 µg / kg for multiple days. In another implementation, the daily dose is a dose in the range of about 5 µg / kg to about 500 µg / kg. In yet another implementation, the daily dose is about 10 µg / kg to about 250 µg / kg. In yet another implementation, the daily dose is about 25 µg / kg to about 150 µg / kg. A preferred dose is about 10 µg / kg. The daily dose can be administered once per day or divided into subdoses and administered in multiple doses, e.g., twice, three times, or four times per month. To achieve the desired therapeutic effect, compositions described herein may be administered for multiple days at the therapeutically effective dose. Thus, therapeutically effective administration of a pharmaceutical composition for use as an HPV vaccine described herein in a subject requires periodic (e.g., daily) administration that continues for a period ranging from once to several months at a weekly basis or longer. Typically, a pharmaceutical composition of a T cell immunogen will be administered for weekly, often for at least six consecutive weeks. While consecutive weekly doses are a preferred route to achieve a therapeutically effective dose, a therapeutically beneficial effect can be achieved even if the pharmaceutical compositions are not administered daily, so long as the administration is repeated frequently enough to maintain a therapeutically effective concentration of the T cell immunogen composition in the subject. For example, one can administer a pharmaceutical composition every other week, every third week, or, if higher dose ranges are employed and tolerated by the subject, once a month. A preferred dosing schedule, for example, can include administering weekly for several months, one week off and repeating this cycle dosing schedule for 3-4 cycles. Optimum dosages, toxicity, and therapeutic efficacy of a pharmaceutical composition described herein may vary depending on the relative potency of individual T cell immunogens and can be determined by standard pharmaceutical procedures in cell cultures or experimental animals. T cell immunogen compositions that exhibit large therapeutic indices are preferred. While compositions that exhibit toxic side effects can be used, care should be taken to design a delivery system that targets vaccine-induced immune responses to HPV infected cells to minimize potential damage to normal cells and, thereby, reduce side effects. Following successful treatment, it may be desirable to have the subject undergo maintenance therapy to prevent the recurrence of the condition or disease treated. As can be appreciated from the disclosure above, the present invention has a wide variety of applications. The invention is further illustrated by the following examples, which are only illustrative and Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT are not intended to limit the definition and scope of the invention in any way. Example 1: MUNIS Identification of Optimal HPV T cell Epitopes The presentation module of MUNIS uses a bi-directional LSTM26, which is fed the peptide sequence as a 1-hot encoded amino acids, including its left and right flanks, corresponding to 5 amino acids to the left and to the right of the peptide in its parent protein sequence of origin. To allow the network to determine which of the amino acids belong to the peptide sequence and not to the flanks, a binary feature is included at each amino acid position. The output of the LSTM is a sequence of vectors, which is pooled into a single vector representation for the sequence by averaging along the sequence length dimension. Finally, this feature vector is concatenated with the one from the binding module and fed into a 2 layer feed- forward network to produce the presentation score. MUNIS deep-learning algorithm outperformed state-of-the-art predictors in classifying HLA class I binders (FIG.3A – FIG.3D). For application to the HPV proteome, consensus sequences of HPV16 and 18 E1, E2, E5, E6 and E7 proteins by aligning all available sequences from the National Center for Biotechnology Information (NCBI). The resulting consensus sequences were verified to exist in the NCBI database. MUNIS was then applied to each of these consensus protein sequences for 40 HLA class I alleles to obtain a list of predicted T cell epitopes with a presentation score greater than 0.95 as depicted in FIG.5. Each of these epitopes were visually mapped to determine regions enriched for T cell epitopes herein referred to as immunologically active for each HPV16 and 18 protein as depicted in Table 2. Example 2: This approach consists of protein network construction and protein network analysis. For network construction, two approaches were used to infer interactions between individual atoms of amino acid residues: an energetic network and a centroid network. In the energetic network, non-covalent interactions, which include van der Waals interactions, hydrogen bonds, water-bridged bonds, salt bridges, disulfide bonds, pi-pi interactions, pi-cation interactions and metal coordinated bonds, were calculated between pairs of residues based on energy potentials and appropriate angle and distance thresholds using the atomic coordinates found in the Protein Data Bank file (PDB Protein networks were then constructed by defining each individual amino acid residue within the protein structure as a node and defining weighted edges as the sum of all intermolecular bond energies between residues. Energies for each bond type were defined using previously established values in kJ / mol. For the centroid network, the side chain center of mass for each amino acid residue and defined bonds based on a distance threshold cutoff between centroids of 8.5 angstroms. The purpose of including the centroid network was to account for the contribution of hydrophobic packing to protein folding. Centroid protein networks were then constructed by defining each amino acid residue as a node and defining edges as binary interactions that meet the defined 8.5 angstrom threshold for centroid-to-centroid distance. Edges to immediately neighboring amino acids (n-1, n+1) were not included in either approach due to presence of covalent peptide bonds between these residues. All calculations were carried out in Python. For protein network analysis, a number filters was applied to calculate network parameters. First, in the energetic network, all edges were considered as well as those strictly between terminal atoms, as previously described, in order to focus on residue-specific interactions. Thus, for an edge to be included, Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT one of the two participating atoms needed to be a terminal atom. Edges were then summed over an amino acid residue to transform the edge list from a list of atom-atom interactions to a list of residue- residue interactions. Second, a filter to calculate network parameters on edges that bridge residues from different higher order protein structures was applied. Higher order protein structures were identified in two ways. First, classical secondary structure was utilized using the publicly available software tool Stride. Second, network-defined higher order structures were inferred based on a random walk approach whereby tightly connected communities are identified and distinguished (Walktrap). For higher order structure filters, no edges were considered between residues within the same structural motif. Together, these filters were used to calculate three network parameters prior to summation of the final network score. The network parameters are as follows: 1. Second Order Intermodular Degree: the number of second order interactions (two degrees of separation) between residues from different higher order structures, as an average of classical secondary structure and Walktrap definitions. where a node has n neighbors in different modules and kiand ksiare the degrees (number of edges) of those neighbors i for the regular energetic network and the terminal atom filtered energetic network, respectively, with higher order structures defined by secondary structure. These values are summed for neighbors 1 through n. If multimeric protein structure data were available, this metric was considered only for the multimer prior to normalization. These calculations were then calculated for the centroid network, where modules defined by both secondary structure (ki) and Walktrap (wi) were used. Each individual value (ki, ksi, wi) was standard normalized before summing. The final SD value was then obtained for each amino acid in the network as an average of the 4 described calculations. The purpose of taking an average of 4 different estimates of second order intermodular degree was to capture the unique contributions of the energetic network, the terminal atom filter, the coarse-grained centroid network and the Walktrap higher order structure definition. 2. Node Edge Betweenness: the summed frequency that a node’s edges were utilized as a shortest path between all pairs of nodes in the network, weighted by edge weight = 1 if edge ejkis used in the shortest path between nodes j and k, otherwise ejk= 0. Only edges between nodes of different higher order structure were allowed, and here the structures were defined by secondary structure. These counts were then summed for all pairs of nodes 1 through n. This edge parameter is then converted into a node parameter: Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT where EB was the edge betweenness for each edge i for a node with n neighbors and EBS was the same metric but for the network filtered on sidechain interactions. These metrics are standard normalized and then averaged. If a multimeric version of the protein exists, then the maximum node edge betweenness is taken between the monomeric and multimeric conformations. 3. Euclidean Distance from Centroid to Ligand: the distance in angstroms of a residue’s centroid to the center of mass of the protein’s ligand. Centroid was defined as the center of mass of a residue’s sidechain, weighted by atomic weight, as described previously: where axis the atomic weight for atom x in a protein’s sidechain for atoms 1 through s. The (x,y,z) 3-dimensional coordinates were defined in the PDB file. The center of mass of the ligand was calculated using all atoms. The final centroid value was standard normalized and averaged. Final network score was a sum of the aforementioned terms, which had been individually normalized: SD + NEB − LD = final network score These values were calculated in R with the assistance of the iGraph package to load networks. PDB Structures: For the validation dataset, the following PDB files were used: Calculation of Network Scores for Multimeric Proteins: For multimeric proteins, degree-based network values (second order degree, ligand binding) in the protein’s highest oligomeric state were utilized prior to calculation of a normalized Z-score. For node edge betweenness metrics, the maximum normalized Z-score from monomer, multimeric or inter- multimeric conformations was incorporated into the final network score calculation. Mutated residues engineered to stabilize protein conformations (e.g.5HGL, Cys14 and Cys45, engineered disulfide bond) were excluded from the analysis. For analyses with multiple structures utilized to capture different conformational states for the same oligomeric structure (e.g.5HGL and 5HGN, open and closed conformations), network Z-scores were averaged. All molecular assemblies were generated using the online server Protein Data Bank in Europe - Proteins, Interfaces, Structures and Assemblies (PDBePISA). Correlation of Network Scores with Functional Datasets: Composite network scores were correlated against functional datasets obtained from high and low-throughput mutagenesis studies. For Temoneira-1 (TEM-1) Beta-lactamase, network scores were correlated against functional mutant values obtained from the Ampicillin 2500 µg / mL dataset, which was the maximum concentration utilized in the study. For DNA methylase Haemophilus aegyptius restriction endonuclease III (HaeIII), correlations were made using the dataset after the full 17 rounds of mutagenesis. For Nonstructural protein 5A (NS5A), the dataset for the virus under selection was analyzed with Daclatasvir. For Kanamycin Kinase, the 1:8 Kanamycin dilution dataset was used. For the remaining proteins, the single supplementary datasets provided were utilized for correlative studies. Each set of functional scores for a given protein was standard normalized by subtracting the mean and dividing by the standard deviation. Calculation of Shannon Entropy: Multiple sequence alignments were downloaded from PFAM. Using the protein sequence derived from the protein’s PDB structure as a reference in each protein sequence alignment, amino acid frequencies were tabulated at each amino acid position in the Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT corresponding aligned orthologous proteins. Shannon entropy H(p) was calculated based on the following formula: H(p) = − Σa pa log2 (pa) where pais the proportion of amino acid a at a given position and qais the background frequency of amino acid a. Residues with uncertain alignment per Protein Family Database (PFAM) were excluded from downstream analyses. The background frequencies used were the frequencies of each amino acid across the entire alignment. Calculation of Relative Solvent Accessibility: Relative Solvent Accessibility (RSA) values were calculated by using the following formula: RSA = Accessible Solvent Area (ASA) / Maximum ASA, with ASA values calculated using the publicly available software tool Stride and utilizing previously reported Maximum ASA values. Receiver Operator Curves: Receiver Operator Curves (ROC) were plotted and calculated in R using the pROC library to determine the predictive ability of network scores, Shannon entropy and relative solvent accessibility values to determine the top 10% of residues ranked by mutational intolerance. Calculation of covariance (CoV) Sequence Entropy: Values for CoV sequence entropy were obtained from the NCBI Virus Sequence Database. For generation of network scores for HPV16 and 18, structure-based network analysis was applied to homology modeling structures of HPV16 and 18 E1, E2, E5, E6 and E7 generated using RoseTTAFold. Network scores from individual amino acid residues within and neighboring a CD8+ T cell epitope were combined and averaged based on their involvement as either an HLA anchor, T-cell receptor (TCR) contact or peptide processing residues. HLA anchor residues were defined based on previous delineations for each HLA allele. Putative TCR contact residues were considered to be all remaining non-HLA anchor residues, excluding position 1, based on previously reported frequencies of TCR-peptide contacts. Flanking residues were defined as the five residues N-terminal and C-terminal to the epitope (ten in total). These three quantities were then summed to generate an overall composite network score for each CD8+ T cell epitope. The normalized epitope network score was calculated by subtracting the lowest epitope network score from all epitope scores, such that all values were greater than or equal to zero. The normalized network score was utilized when comparing patient responses such that no cytotoxic T lymphocytes (CTL) response would be assigned a negative value. Example 3: Multi-Epitope Vaccine for Therapeutic HPV Clearance In this Example, an HPV cell-based immunogen was developed that incorporates mutation- constrained and / or immunogenically active T cell epitope fragments that have been identified by MUNIS and through an algorithm known as structure-based network analysis algorithm as depicted in Table 2. Regions that lacked any epitopes served as natural stops or breaks within each protein sequence to delineate new fragments for vaccine cassette inclusion. In cases where protein functional domains were still intact and contained no immunogenically active regions, the domains were split into two fragments containing a 9 amino acid overlap to conserve any CD8 epitopes that may span these regions while ablating the domains structural and functional properties, such as splitting a zinc finger domain of HPV16 E6 in half to remove oncogenic properties but retain native immunogenic CD8 T cell epitopes. In a few cases, conservative mutations to the amino acid sequence were made to remove highly probable splice acceptor and donor sites from DNA-based constructs. These mutations are outlined in red and summarized in Table 2. In some cases, the fragments listed have a “#.2” denotation, meaning they Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT are a shortened version of the parent fragment for use in the combined HPV16 and 18 vaccines to reduce the size of the cassette. The immunologically active and highly networked HPV 16 and / or 18 fragments from Table 2 were linked directly in difference embodiments to one another with a linker, such as alanine, alanine, tyrosine (AAY) or furin cleavage site such as RGRRKRS (SEQ ID NO: 655). For vaccine constructs with furin cleavage sites, the N-terminus was an endoplasmic reticulum insertion signal sequence (ERISS). For constructs with both AAY and furin cleavage sites, a C-terminus universal tetanus-diphtheria CD4+ T cell helper epitope was also placed. Example 4: Assessment of mRNA Immunogenicity To assess the immunogenicity of candidate HPV T cell vaccines, six (6) cassettes comprised of combinations of immunogenic fragments described herein above in Table 2 were expressed as mRNA molecules and encapsulated in lipid nanoparticles (LNP). These six cassettes were: 1) HPV16 E1-E7 Fragment ERISS Furin (16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, 16E7 F3); 2) HPV16 E1-E7 Fragment AAY (16E1 F2, 16E1 F3, 16E1 F4, 16E1 F5, 16E1 F6, 16E1 F7, 16E1 F8, 16E1 F9, 16E1 F10, 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6, 16E2 F7, 16E5 F1, 16E6 F1, 16E6 F2, 16E6 F3, 16E7 F1, 16E7 F2, 16E7 F3); 3) HPV18 E1-E7 Fragment ERISS Furin (18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 E4, 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3); 4) HPV18 E1-E7 Fragment AAY (18E1 F1, 18E1 F2, 18E1 F3, 18E1 F4, 18E1 F5, 18E1 F6, 18E1 F7, 18E1 F8, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 E4, 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3); 5) HPV16 / 18 E1-E7 Fragment ERISS Furin (16E1 F1, 16E1 F2, 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6.2, 16E5 F1, 16E6 F1, 16E6 F2.2, 16E6 F3, 16E7 F1, 16E7 F2.2, 16E7 F3.2, 18E1 F1.2, 18E1 F2.2, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 E4, 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3); and 6) HPV16 / 18 E1-E7 Fragment AAY (16E1 F1, 16E1 F2, 16E2 F1, 16E2 F2, 16E2 F3, 16E2 F4, 16E2 F5, 16E2 F6.2, 16E5 F1, 16E6 F1, 16E6 F2.2, 16E6 F3, 16E7 F1, 16E7 F2.2, 16E7 F3.2, 18E1 F1.2, 18E1 F2.2, 18E2 F1, 18E2 F2, 18E2 F3, 18E2 E4, 18E2 F5, 18E5 F1, 18E6 F1, 18E6 F2, 18E6 F3, 18E7 F1, 18E7 F2, 18E7 F3). To form the LNPs, an ethanol organic phase containing four lipids and a 20 mM acetate buffer aqueous phase containing the mRNAs were fed into a microfluidics chip through separate mixing channels. The phase ratio (aqueous:organic phase) was adjusted using the computer interface of the machine at 3:1 respectively with a total flow rate of 4 ml / min. The encapsulated LNP product was collected under 60s and immediately subjected to a quench step using IX PBS, followed by ultracentrifugation using 10kD Amicon filters for ethanol removal and buffer exchange. After ultracentrifugation, sucrose was added to the final collected product, followed by sterile filtration using a 0.22 µm polyethersulfone (PES) filter. Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT These LNP-mRNA vaccines were then delivered across two experiments to C57Bl / 6 mice (n=5 per group) at an initial prime dose of 10 µg (day 0) and then a boost of 10 µg (day 21). Animals were then taken down on day 28 and spleens were harvested to assess vaccine-induced T cell responses by IFN-γ ELISpot and intracellular cytokine staining of IFN-γ and TNF-α following stimulation with HPV-specific overlapping 15mer peptide pools derived from HPV16 and HPV18 proteins E1, E2, E5, E6 and E7. For the first experiment, HPV16 containing vaccines were tested (HPV16 E1-E7 Fragment ERISS Furin, HPV16 E1-E7 Fragment AAY, HPV16 / 18 E1-E7 Fragment ERISS Furin and HPV16 / 18 E1-E7 Fragment AAY). This revealed that all four (4) LNP-mRNA vaccines were able to successfully induce T cell responses specific for HPV16 peptide pools as determined by IFN-γ ELISpot (FIG.6A – FIG.6C) and intracellular cytokine staining (FIG.7A – FIG.7C). The HPV16 E1-E7 Fragment AAY cassette appeared to induce the strongest responses to HPV16 E1 pool and HPV16 optimal peptide pool, suggesting it may be an optimal cassette design. In addition, the HPV16 E1-specific responses were also cross-reactive to the HPV35 E1 overlapping peptide pool (FIG.6A – FIG.6C and FIG.7A – FIG.7C), indicating that these vaccines could also be therapeutic for HPV35 as well. Interestingly, the HPV16 / 18 E1-E7 Fragment AAY vaccine was also able to induce responses to the HPV16 E2 / E5 peptide pool (FIG.6A – FIG.6C and FIG. 7A – FIG.7C). For the second experiment, HPV18 containing vaccines were tested (HPV18 E1-E7 Fragment ERISS Furin, HPV18 E1-E7 Fragment AAY, HPV16 / 18 E1-E7 Fragment ERISS Furin and HPV16 / 18 E1- E7 Fragment AAY). Similar to the HPV16 vaccines, it was determined that that all four (4) HPV18 LNP- mRNA vaccines were immunogenic as demonstrated by reactivity of T cells to HPV18 peptide pools by both IFN-γ ELISpot and intracellular cytokine staining (FIG.8A – FIG.8C). The HPV18 E1-E7 Fragment AAY cassette appeared to induce the strongest responses to HPV18 E1 pool, E6 pool, E7 pool and HPV18 E6 KI9 optimal peptide, suggesting it may be an optimal cassette design for HPV18. In addition, the HPV18 E1- and E6- specific responses were also cross-reactive to the HPV45 E1 and E6 peptide pool (FIG.8A – FIG.8C and FIG.9A – FIG.9C), indicating that these vaccines could also be therapeutic for HPV45 as well. Overall, these studies demonstrate that these HPV16 and 18 vaccine cassettes are immunogenic when formulated as LNP-mRNAs. Example 5: Assessment of Chimpanzee Adenoviral (ChAd) HPV Immunogenicity Replication-deficient Chimpanzee Adenoviral (ChAd) vectors were designed to assess immunogenicity of HPV immunogens when synthesized as ChAd vectors. The primary genome was based on Simian Adenovirus 25 (SAdV-25) (NCBI Reference Sequence: AC_000011.1). SAdV-25 was retrieved from ATCC and its genomic DNA was extracted. Sequencing revealed 5-6 SNPs in the genome of the strain obtained from ATCC that differed from the NCBI published sequence. For the E4 modifications for the vector being tested in this application, part of the Human adenovirus type 5 strain NHRC Ad5FS 7151 (HAdV-5) E4 ORF6 gene was amplified and inserted into the SAdV-25 genome. This region has the coordinates of 33172 – 34081 in this specific HAdV-5 genome (NCBI Sequence ID: AY601635.1). The HAdV-5 E4 ORF6 sequence that was inserted had two polymorphisms compared to the HAdV-5 sequence on NCBI and this region was inserted in between coordinates 33704 – 36106 in the SAdV-25 sequence. One of skill in the art could make these or similar modifications. The E1 and E3 Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT genes were deleted from SAdV-25, as well. Immunogen cassettes were then cloned into the E1 region. Tested immunogen cassettes include: HPV16 E1-E7 Fragments, AAY; HPV16 E1-E7 Fragments, ERISS- Furin; HPV16 / 18 E1-E7 Fragments, ERISS-Furin; HPV18 E1-E7 Fragments, AAY. C57BL / 6 mice were vaccinated with the above HPV T cell ChAd vaccines at a dose of 1x109viral particles (or 100 µL PBS for the control group).21 days later, the mice were euthanized, and spleens were harvested to assess vaccine induced T cell responses. Intracellular cytokine staining and ELISpot experiments were conducted in the same format as described above. Similar to the mRNA vaccine results, the ChAd vaccines containing only HPV16 fragments (HPV16 E1-E7 Fragments, AAY; HPV16 E1-E7 Fragments, ERISS-Furin) were able to induce T cell responses specific for HPV16 peptide pools as determined by IFN-γ ELISpot (FIG.10A) and intracellular cytokine staining confirmed that these responses were primarily CD8+T cells (FIG.10B). The strongest responses were to HPV16 E1 pool. The magnitude of responses between the HPV16 E1-E7 Fragments, AAY and HPV16 E1-E7 Fragments, ERISS-Furin vaccines were also similar, suggesting AAY and Furin linkers may have comparable immunogenicity in this context. As seen with the mRNA vaccines, these constructs in ChAd vectors also produced cross-reactive T cell responses to the HPV35 E1 pool (FIG. 10A), indicating that these vaccines could also be a therapeutic option for HPV35 as well. In the ChAd vector, the HPV16 / 18 E1-E7 Fragments, ERISS-Furin and HPV18 E1-E7 Fragments, AAY constructs were able to induce T cell responses specific to HPV18 peptide pools as determined by IFN-γ ELISpot assays (FIG.11A). Both vaccines induced detectable responses to the HPV18 E6 KI9 peptide, while the HPV18 E1-E7 Fragments, AAY vaccine generated additional responses to the HPV18 E1 pool and HPV18 E6 pool. Intracellular cytokine staining confirmed these responses were primarily driven by CD8+T cells although some CD4+T cell response is also detected to the HPV18 E1 Pool (FIG.11B). Further, the HPV18 E1-E7 Fragments, AAY vaccine induced cross-reactive T cell responses to HPV45 E1 pool and HPV45 E6 pool, suggesting this vaccine could also be therapeutic for HPV45 as well. Overall, these studies demonstrate that these HPV16 and 18 vaccine cassettes are immunogenic when formulated as chimpanzee adenoviral vectors. For ELISpot assays shown in FIG.10A, FIG.10B, FIG.11A, and FIG.11B, 500,000 splenocytes were plated per well and stimulated with peptide pools at a concentration of 100 ng / mL per peptide for 14 hours. Peptide pools were overlapping peptide pools made of 15-mers with 11 amino acids of overlap. For intracellular cytokine staining (ICS) shown in FIG.10B and FIG.11B, 600,000 cells were plated and stimulated for 5 hours (4 hours in the presence of golgi plug). ICS was performed, staining for CD3, CD4, CD8, TNF-α and IFN-γ. Peptide pools were overlapping peptide pools made of 15-mers with 11 amino acids of overlap. Example 6: Assessment of mRNA Immunogenicity in HLA-A*02:01 Knock-In Mice To assess the immunogenicity of the HPV16 E1-E7 Fragments, AAY LNP-mRNA T cell vaccine (the same vaccine described in Example 4) in a more human immune context, an HLA-A*02:01 knock-in mouse model that solely expresses the HLA-A*0201 alleles and is devoid of mouse MHC class I was utilized. The HPV16 E1-E7 Fragments AAY linker LNP-mRNA vaccine was delivered to HLA-A*02:01 knock-in mice (n=5) at an initial prime dose of 5 µg (day 0) and then a boost of 5 µg (day 14), or 100 uL Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT PBS on each day for the control group (n=3). Twenty-one days post-vaccination, the mice were euthanized and spleens were harvested to assess vaccine-induced T cell responses. Intracellular cytokine staining and ELISpot experiments were conducted in the same manner as described above. Peptide pools for stimulation contained MUNIS-predicted and IEDB-deposited CD8+T cell epitopes for HLA-A*02:01 present in the vaccine and were separated by HPV16 early proteins (i.e. HPV16 E1 pool, HPV16 E2 pool, etc.). The HPV16 E1-E7 Fragments, AAY LNP-mRNA vaccine induced T cell responses to HPV16 E1 pool and HPV16 E7 pool (FIG.12A), which were confirmed to be primarily CD8+T cell responses via ICS (FIG.12B). When the responses within the HPV16 E7 Pool were mapped, it was found that the vaccine induced responses to the established HLA-A*02 peptide YMLDLQPET (SEQ ID NO: 411) (YT9) (FIG.12A and FIG.12B). HPV16 E7 YT9 is a MUNIS-predicted HLA-A*02:01 epitope that has also previously been deposited on IEDB. When the responses within the HPV16 E1 Pool were mapped, it was found the vaccine induced T cell responses to a novel epitope, CLYLHIQSL (SEQ ID NO: 107) (CL9) (FIG.12A). HPV16 E1 CL9 is a MUNIS-predicted HLA-A*02:01 epitope, not previously deposited in IEDB or identified and is therefore novel to the best of our knowledge. Overall, these studies demonstrate that the HPV16 vaccine cassette is immunogenic in HLA-A*0201 knock-in mice and can induce both established and novel HLA-A*0201-restricted epitopes. For ELISpot assays shown in FIG.12A and FIG.12B, 500,000 splenocytes were plated per well and stimulated with 1 µM per peptide for 14 hours. Peptide pools contained MUNIS-predicted and IEDB- deposited CD8+ T cell epitopes present in the vaccine. For intracellular cytokine staining (ICS) shown in FIG.12B, 600,000 cells were plated and stimulated for 5 hours (4 hours in the presence of golgi plug). ICS was performed, staining for CD3, CD4, CD8, TNF-α and IFN-γ. Peptide pools contained MUNIS- predicted and IEDB-deposited CD8+ T cell epitopes present in the vaccine. Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, the descriptions and examples should not be construed as limiting the scope of the invention. The disclosures of all patent and scientific literature cited herein are expressly incorporated in their entirety by reference. REFERENCES 1. Collins, D.R., Gaiha, G.D., and Walker, B.D. (2020). CD8+ T cells in HIV control, cure and prevention. Nat. Rev. Immunol.20, 471–482.10.1038 / s41577-020-0274-9. 2. Arunachalam, P.S., Charles, T.P., Joag, V., Bollimpelli, V.S., Scott, M.K.D., Wimmers, F., Burton, S.L., Labranche, C.C., Petitdemange, C., Gangadhara, S., et al. (2020). T cell-inducing vaccine durably prevents mucosal SHIV infection even with lower neutralizing antibody titers. Nat. Med.26, 932– 940.10.1038 / s41591-020-0858-8. 3. Bhattacharyya, S., Crain, C.R., Goldberg, B., and Gaiha, G.D. (2023). Features of functional and dysfunctional CD8+ T cells to guide HIV vaccine development. Curr. Opin. HIV AIDS 18, 257–263. 10.1097 / COH.0000000000000812. 4. Moss, P. (2022). The T cell immune response against SARS-CoV-2. Nat. Immunol.23, 186– 193.10.1038 / s41590-021-01122-w. 5. Clemens, E.B., van de Sandt, C., Wong, S.S., Wakim, L.M., and Valkenburg, S.A. (2018). Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT Harnessing the Power of T Cells: The Promising Hope for a Universal Influenza Vaccine. Vaccines 6, 18. 10.3390 / vaccines6020018. 6. Welsh, R.M., and Fujinami, R.S. (2007). Pathogenic epitopes, heterologous immunity and vaccine design. Nat. Rev. Microbiol.5, 555–563.10.1038 / nrmicro1709. 7. Yewdell, J.W., and Bennink, J.R. (1999). Immunodominance in Major Histocompatibility Complex Class I–Restricted T Lymphocyte Responses. Annu. Rev. Immunol.17, 51–88. 10.1146 / annurev.immunol.17.1.51. 8. Reynisson, B., Alvarez, B., Paul, S., Peters, B., and Nielsen, M. (2020). NetMHCpan-4.1 and NetMHCIIpan-4.0: improved predictions of MHC antigen presentation by concurrent motif deconvolution and integration of MS MHC eluted ligand data. Nucleic Acids Res.48, W449– W454. 10.1093 / nar / gkaa379. 9. O’Donnell, T.J., Rubinsteyn, A., and Laserson, U. (2020). MHCflurry 2.0: Improved Pan- Allele Prediction of MHC Class I-Presented Peptides by Incorporating Antigen Processing. Cell Syst.11, 42-48.e7.10.1016 / j.cels.2020.06.010. 10. Sarkizova, S., Klaeger, S., Le, P.M., Li, L.W., Oliveira, G., Keshishian, H., Hartigan, C.R., Zhang, W., Braun, D.A., Ligon, K.L., et al. (2020). A large peptidome dataset improves HLA class I epitope prediction across most of the human population. Nat. Biotechnol.38, 199–209.10.1038 / s41587- 019-0322-9. 11. Gfeller, David, et al. "Improved predictions of antigen presentation and TCR recognition with MixMHCpred2.2 and PRIME2.0 reveal potent SARS-CoV-2 CD8+ T-cell epitopes." Cell Systems 14.1 (2023): 72-83. 12. Buckley, P.R., Lee, C.H., Ma, R., Woodhouse, I., Woo, J., Tsvetkov, V.O., Shcherbinin, D.S., Antanaviciute, A., Shughay, M., Rei, M., et al. (2022). Evaluating performance of existing computational models in predicting CD8+ T cell pathogenic epitopes and cancer neoantigens. Brief. Bioinform.23, bbac141.10.1093 / bib / bbac141. 13. Calis, J.J.A., Maybeno, M., Greenbaum, J.A., Weiskopf, D., Silva, A.D.D., Sette, A., Keşmir, C., and Peters, B. (2013). Properties of MHC Class I Presented Peptides That Enhance Immunogenicity. PLOS Comput. Biol.9, e1003266.10.1371 / journal.pcbi.1003266. 14. Schmidt, J., Smith, A.R., Magnin, M., Racle, J., Devlin, J.R., Bobisse, S., Cesbron, J., Bonnet, V., Carmona, S.J., Huber, F., et al. (2021). Prediction of neo-epitope immunogenicity reveals TCR recognition determinants and provides insight into immunoediting. Cell Rep. Med.2, 100194. 10.1016 / j.xcrm.2021.100194. 15. Rives, A., Meier, J., Sercu, T., Goyal, S., Lin, Z., Liu, J., Guo, D., Ott, M., Zitnick, C.L., Ma, J., et al. (2021). Biological structure and function emerge from scaling unsupervised learning to 250 million protein sequences. Proc. Natl. Acad. Sci.118, e2016239118.10.1073 / pnas.2016239118. 16. Racle, J., Guillaume, P., Schmidt, J., Michaux, J., Larabi, A., Lau, K., Perez, M.A.S., Croce, G., Genolet, R., Coukos, G., et al. (2023). Machine learning predictions of MHC-II specificities reveal alternative binding mode of class II epitopes. Immunity 56, 1359-1375.e13. 10.1016 / j.immuni.2023.03.009. 17. Stražar, M., Park, J., Abelin, J.G., Taylor, H.B., Pedersen, T.K., Plichta, D.R., Brown, E.M., Eraslan, B., Hung, Y.-M., Ortiz, K., et al. (2023). HLA-II immunopeptidome profiling and deep learning Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT reveal features of antigenicity to inform antigen discovery. Immunity 56, 1681- 1698.e13. 10.1016 / j.immuni.2023.05.009. 18. Kaseke, C., Park, R.J., Singh, N.K., Koundakjian, D., Bashirova, A., Garcia Beltran, W.F., Takou Mbah, O.C., Ma, J., Senjobe, F., Urbach, J.M., et al. (2021). HLA class-I-peptide stability mediates CD8+ T cell immunodominance hierarchies and facilitates HLA-associated immune control of HIV. Cell Rep.36, 109378.10.1016 / j.celrep.2021.109378. 19. Smatti, M.K., Al-Sadeq, D.W., Ali, N.H., Pintus, G., Abou-Saleh, H., and Nasrallah, G.K. (2018). Epstein–Barr Virus Epidemiology, Serology, and Genetic Variability of LMP-1 Oncogene Among Healthy Population: An Update. Front. Oncol.8, 211.10.3389 / fonc.2018.00211. 12. Bruno, P.M., Timms, R.T., Abdelfattah, N.S., Leng, Y., Lelis, F.J.N., Wesemann, D.R., Yu, X.G., and Elledge, S.J. (2023). High-throughput, targeted MHC class I immunopeptidomics using a functional genetics screening platform. Nat. Biotechnol.41, 980–992.10.1038 / s41587- 022-01566-x. 21. Vita, R., Mahajan, S., Overton, J.A., Dhanda, S.K., Martini, S., Cantrell, J.R., Wheeler, D.K., Sette, A., and Peters, B. (2019). The Immune Epitope Database (IEDB): 2018 update. Nucleic Acids Res. 47, D339–D343.10.1093 / nar / gky1006. 22. Rives, Alexander, et al. "Biological structure and function emerge from scaling unsupervised learning to 250 million protein sequences." Proceedings of the National Academy of Sciences 118.15 (2021): e2016239118. 23. Gao A, Chen Z, Segal FP, Carrington M, Streeck H, Chakraborty AK, Julg B. Predicting the Immunogenicity of T cell epitopes: From HIV to SARS-CoV-2. bioRxiv [Preprint].2020 May 15:2020.05.14.095885. doi: 10.1101 / 2020.05.14.095885. Update in: iScience.2021 Apr 23;24(4):102311. PMID: 32511339; PMCID: PMC7241102. 24. Streeck, H., Jolin, J. S., Qi, Y., Yassine-Diab, B., Johnson, R. C., Kwon, D. S., ... & Altfeld, M. (2009). Human immunodeficiency virus type 1-specific CD8+ T-cell responses during primary infection are major determinants of the viral set point and loss of CD4+ T cells. Journal of virology, 83(15), 7641-7648. 25. Kingma, Diederik P. and Jimmy Ba. “Adam: A Method for Stochastic Optimization.” CoRR abs / 1412.6980 (2014): n. pag. 26. Hochreiter, S., & Schmidhuber, J. (1997). Long short-term memory. Neural computation, 9(8), 1735-1780. 27. Bairoch, Amos, and Rolf Apweiler. "The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000." Nucleic acids research 28.1 (2000): 45-48. 28. Zeming Lin et al. ,Evolutionary-scale prediction of atomic-level protein structure with a language model. Science.379,1123-1130(2023).DOI:10.1126 / science.ade2574 29. Maria Hauser, Martin Steinegger, Johannes Söding, MMseqs software suite for fast and deep clustering and searching of large protein sequence sets, Bioinformatics, Volume 32, Issue 9, May 2016, Pages 1323–1330. 30. Robinson J, Barker DJ, Georgiou X, Cooper MA, Flicek P, Marsh SGE. IPD-IMGT / HLA Database. Nucleic Acids Res.2020 Jan 8;48(D1):D948-D955. doi: 10.1093 / nar / gkz950. PMID: 31667505; PMCID: PMC7145640.

Claims

Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT CLAIMS Having described the invention, we claim:

1. A multi-epitope T cell immunogen composition comprising two or more Human Papilloma Virus (HPV) epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to an HPV epitope in FIG.

5.

2. The multi-epitope T cell immunogen composition of claim 1, wherein the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to the selected HPV epitope are (SEQ ID NO: 107), (SEQ ID NO: 449), (SEQ ID NO: 1), (SEQ ID NO: 2), (SEQ ID NO: 3), (SEQ ID NO: 4), (SEQ ID NO: 5), (SEQ ID NO: 6), (SEQ ID NO: 7), (SEQ ID NO: 8), (SEQ ID NO: 9), (SEQ ID NO: 10), (SEQ ID NO: 11), (SEQ ID NO: 12), (SEQ ID NO: 13), (SEQ ID NO: 14), (SEQ ID NO: 15), (SEQ ID NO: 16), (SEQ ID NO: 17), (SEQ ID NO: 18), (SEQ ID NO: 19), (SEQ ID NO: 20), (SEQ ID NO: 21), (SEQ ID NO: 22), (SEQ ID NO: 23), (SEQ ID NO: 24), (SEQ ID NO: 25), (SEQ ID NO: 26), (SEQ ID NO: 27), (SEQ ID NO: 28), (SEQ ID NO: 29), (SEQ ID NO: 30), (SEQ ID NO: 31), (SEQ ID NO: 32), (SEQ ID NO: 33), (SEQ ID NO: 34), (SEQ ID NO: 35), (SEQ ID NO: 36), (SEQ ID NO: 37), (SEQ ID NO: 38), (SEQ ID NO: 39), (SEQ ID NO: 40), (SEQ ID NO: 41), (SEQ ID NO: 42), (SEQ ID NO: 43), (SEQ ID NO: 44), (SEQ ID NO: 45), (SEQ ID NO: 46), (SEQ ID NO: 47), (SEQ ID NO: 48), (SEQ ID NO: 49), (SEQ ID NO: 50), (SEQ ID NO: 51), (SEQ ID NO: 52), (SEQ ID NO: 53), (SEQ ID NO: 54), (SEQ ID NO: 55), (SEQ ID NO: 56), (SEQ ID NO: 57), (SEQ ID NO: 58), (SEQ ID NO: 59), (SEQ ID NO: 60), (SEQ ID NO: 61), (SEQ ID NO: 62), (SEQ ID NO: 63), (SEQ ID NO: 64), (SEQ ID NO: 65), (SEQ ID NO: 66), (SEQ ID NO: 67), (SEQ ID NO: 68), (SEQ ID NO: 69), (SEQ ID NO: 70), (SEQ ID NO: 71), (SEQ ID NO: 72), (SEQ ID NO: 73), (SEQ ID NO: 74), (SEQ ID NO: 75), (SEQ ID NO: 76), (SEQ ID NO: 77), (SEQ ID NO: 78), (SEQ ID NO: 79), (SEQ ID NO: 80), (SEQ ID NO: 81), (SEQ ID NO: 82), (SEQ ID NO: 83), (SEQ ID NO: 84), (SEQ ID NO: 85), (SEQ ID NO: 86), (SEQ ID NO: 87), (SEQ ID NO: 88), (SEQ ID NO: 89), (SEQ ID NO: 90), (SEQ ID NO: 91), (SEQ ID NO: 92), (SEQ ID NO: 93), (SEQ ID NO: 94), (SEQ ID NO: 95), (SEQ ID NO: 96), (SEQ ID NO: 97), (SEQ ID NO: 98), (SEQ ID NO: 99), (SEQ ID NO: 100), (SEQ ID NO: 101), (SEQ ID NO: 102), (SEQ ID NO: 103), (SEQ ID NO: 104), (SEQ ID NO: 105), (SEQ ID NO: 106), (SEQ ID NO: 108), (SEQ ID NO: 109), (SEQ ID NO: 110), (SEQ ID NO: 111), (SEQ ID NO: 112), (SEQ ID NO: 113), (SEQ ID NO: 114), (SEQ ID NO: 115), (SEQ ID NO: 116) (SEQ ID NO: 116), (SEQ ID NO: 117), (SEQ ID NO: 118), (SEQ ID NO: 119), (SEQ ID NO: 120), (SEQ ID NO: 121), (SEQ ID NO: 122), (SEQ ID NO: 123), (SEQ ID NO: 124), (SEQ ID NO: 125), (SEQ ID NO: 126), (SEQ ID NO: 127), (SEQ ID NO: 128), (SEQ ID NO: 129), (SEQ ID NO: 130), (SEQ ID NO: 131), (SEQ ID NO: 132), (SEQ ID NO: 133), (SEQ ID NO: 134), (SEQ ID NO: 135), (SEQ ID NO: 136), (SEQ ID NO: 137), (SEQ ID NO: 138), (SEQ ID NO: 139), (SEQ ID NO: 140), (SEQ ID NO: 141), (SEQ ID NO: 142), (SEQ ID NO: 143), (SEQ ID NO: 144), (SEQ ID NO: 145), (SEQ ID NO: 146), (SEQ ID NO: 147), (SEQ ID NO: 148), (SEQ ID NO: 149), (SEQ ID NO: 150), (SEQ ID NO: 151), (SEQ ID NO: 152), (SEQ ID NO: 153), (SEQ ID NO: 154), (SEQ ID NO: 155), (SEQ ID NO: 156), (SEQ ID NO: 157), (SEQ ID NO: 158), (SEQ ID NO: 159), (SEQ ID NO: 160), (SEQ ID NO: 161), (SEQ ID NO: 162), (SEQ ID NO: 163), (SEQ ID NO: 164), (SEQ ID NO: 165), (SEQ ID NO: 166), (SEQ ID NO: 167), (SEQ ID NO: 168), (SEQ ID NO: 169) (SEQ ID NO: 170), (SEQ ID NO: 171), (SEQ ID NO: 172), (SEQ ID NO: 173), (SEQ IDAttorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT NO: 174), (SEQ ID NO: 175), (SEQ ID NO: 176), (SEQ ID NO: 177), (SEQ ID NO: 178), (SEQ ID NO: 179), (SEQ ID NO: 180), (SEQ ID NO: 181), (SEQ ID NO: 182), (SEQ ID NO: 183), (SEQ ID NO: 184), (SEQ ID NO: 185), (SEQ ID NO: 186), (SEQ ID NO: 187), (SEQ ID NO: 188), (SEQ ID NO: 189), (SEQ ID NO: 190), (SEQ ID NO: 191), (SEQ ID NO: 192), (SEQ ID NO: 193), (SEQ ID NO: 194), (SEQ ID NO: 195), (SEQ ID NO: 196), (SEQ ID NO: 197), (SEQ ID NO: 198), (SEQ ID NO: 199), (SEQ ID NO: 200), (SEQ ID NO: 201), (SEQ ID NO: 202), (SEQ ID NO: 203), (SEQ ID NO: 204), (SEQ ID NO: 205), (SEQ ID NO: 206), (SEQ ID NO: 207), (SEQ ID NO: 208), (SEQ ID NO: 209), (SEQ ID NO: 210), (SEQ ID NO: 211), (SEQ ID NO: 212), (SEQ ID NO: 213), (SEQ ID NO: 214), (SEQ ID NO: 215), (SEQ ID NO: 216), (SEQ ID NO: 217), (SEQ ID NO: 218), (SEQ ID NO: 219), (SEQ ID NO: 220), (SEQ ID NO: 221), (SEQ ID NO: 222), (SEQ ID NO: 223), (SEQ ID NO: 224), (SEQ ID NO: 225), (SEQ ID NO: 226), (SEQ ID NO: 227), (SEQ ID NO: 228), (SEQ ID NO: 229), (SEQ ID NO: 230), (SEQ ID NO: 231), (SEQ ID NO: 232), (SEQ ID NO: 233), (SEQ ID NO: 234), (SEQ ID NO: 235), (SEQ ID NO: 236), (SEQ ID NO: 237), (SEQ ID NO: 238), (SEQ ID NO: 239), (SEQ ID NO: 240), (SEQ ID NO: 241), (SEQ ID NO: 242), (SEQ ID NO: 243), (SEQ ID NO: 244), (SEQ ID NO: 245), (SEQ ID NO: 246), (SEQ ID NO: 247), (SEQ ID NO: 248), (SEQ ID NO: 249), (SEQ ID NO: 250), (SEQ ID NO: 251), (SEQ ID NO: 252), (SEQ ID NO: 253), (SEQ ID NO: 254), (SEQ ID NO: 255), (SEQ ID NO: 256), (SEQ ID NO: 257), (SEQ ID NO: 258), (SEQ ID NO: 259), (SEQ ID NO: 260), (SEQ ID NO: 261), (SEQ ID NO: 262), (SEQ ID NO: 263), (SEQ ID NO: 264), (SEQ ID NO: 265), (SEQ ID NO: 266), (SEQ ID NO: 267), (SEQ ID NO: 268), (SEQ ID NO: 269), (SEQ ID NO: 270), (SEQ ID NO: 271), (SEQ ID NO: 272), (SEQ ID NO: 273), (SEQ ID NO: 274), (SEQ ID NO: 275), (SEQ ID NO: 276), (SEQ ID NO: 277), (SEQ ID NO: 278), (SEQ ID NO: 279), (SEQ ID NO: 280), (SEQ ID NO: 281), (SEQ ID NO: 282), (SEQ ID NO: 283), (SEQ ID NO: 284), (SEQ ID NO: 285), (SEQ ID NO: 286), (SEQ ID NO: 287), (SEQ ID NO: 288), (SEQ ID NO: 289), (SEQ ID NO: 290), (SEQ ID NO: 291), (SEQ ID NO: 292), (SEQ ID NO: 293), (SEQ ID NO: 294), (SEQ ID NO: 295), (SEQ ID NO: 296), (SEQ ID NO: 297), (SEQ ID NO: 298), (SEQ ID NO: 299), (SEQ ID NO: 300), (SEQ ID NO: 301), (SEQ ID NO: 302), (SEQ ID NO: 303), (SEQ ID NO: 304), (SEQ ID NO: 305), (SEQ ID NO: 306), (SEQ ID NO: 307), (SEQ ID NO: 308), (SEQ ID NO: 309), (SEQ ID NO: 310), (SEQ ID NO: 311), (SEQ ID NO: 312), (SEQ ID NO: 313), (SEQ ID NO: 314), (SEQ ID NO: 315), (SEQ ID NO: 316), (SEQ ID NO: 317), (SEQ ID NO: 318), (SEQ ID NO: 319), (SEQ ID NO: 320), (SEQ ID NO: 321), (SEQ ID NO: 322), (SEQ ID NO: 323), (SEQ ID NO: 324), (SEQ ID NO: 325), (SEQ ID NO: 326), (SEQ ID NO: 327), (SEQ ID NO: 328), (SEQ ID NO: 329), (SEQ ID NO: 330), (SEQ ID NO: 331), (SEQ ID NO: 332), (SEQ ID NO: 333), (SEQ ID NO: 334), (SEQ ID NO: 335), (SEQ ID NO: 336), (SEQ ID NO: 337), (SEQ ID NO: 338), (SEQ ID NO: 339), (SEQ ID NO: 340), (SEQ ID NO: 341), (SEQ ID NO: 342), (SEQ ID NO: 343), (SEQ ID NO: 344), (SEQ ID NO: 345), (SEQ ID NO: 346), (SEQ ID NO: 347), (SEQ ID NO: 348), (SEQ ID NO: 349), (SEQ ID NO: 350), (SEQ ID NO: 351), (SEQ ID NO: 352), (SEQ ID NO: 353), (SEQ ID NO: 354), (SEQ ID NO: 355), (SEQ ID NO: 356), (SEQ ID NO: 357), (SEQ ID NO: 358), (SEQ ID NO: 359), (SEQ ID NO: 360), (SEQ ID NO: 361), (SEQ ID NO: 362), (SEQ ID NO: 363), (SEQ ID NO: 364), (SEQ ID NO: 365), (SEQ ID NO: 366), (SEQ ID NO: 367), (SEQ ID NO: 368), (SEQ ID NO: 369), (SEQ ID NO: 370), (SEQ ID NO: 371), (SEQ ID NO: 372), (SEQ ID NO: 373), (SEQ ID NO: 374), (SEQ ID NO: 375), (SEQ ID NO: 376), (SEQ ID NO: 377), (SEQ ID NO: 378), (SEQ ID NO: 379), (SEQ ID NO: 380), (SEQ ID NO: 381), (SEQ ID NO: 382), (SEQ ID NO: 383), (SEQ ID NO: 384), (SEQ ID NO: 385), (SEQ ID NO: 386), (SEQ ID NO: 387), (SEQ ID NO: 388), (SEQ ID NO: 389), (SEQ ID NO: 390), (SEQ ID NO: 391), (SEQ ID NO: 392),Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT (SEQ ID NO: 393), (SEQ ID NO: 394), (SEQ ID NO: 395), (SEQ ID NO: 396), (SEQ ID NO: 397), (SEQ ID NO: 398), (SEQ ID NO: 399), (SEQ ID NO: 400), (SEQ ID NO: 401), (SEQ ID NO: 402), (SEQ ID NO: 403), (SEQ ID NO: 404), (SEQ ID NO: 405), (SEQ ID NO: 406), (SEQ ID NO: 407), (SEQ ID NO: 408), (SEQ ID NO: 409), (SEQ ID NO: 410), (SEQ ID NO: 411), (SEQ ID NO: 412), (SEQ ID NO: 413), (SEQ ID NO: 414), (SEQ ID NO: 415), (SEQ ID NO: 416), (SEQ ID NO: 417), (SEQ ID NO: 418), (SEQ ID NO: 419), (SEQ ID NO: 420), (SEQ ID NO: 421), (SEQ ID NO: 422), (SEQ ID NO: 423), (SEQ ID NO: 424), (SEQ ID NO: 425), (SEQ ID NO: 426), (SEQ ID NO: 427), (SEQ ID NO: 428), (SEQ ID NO: 429), (SEQ ID NO: 430), (SEQ ID NO: 431), (SEQ ID NO: 432), (SEQ ID NO: 433), (SEQ ID NO: 434), (SEQ ID NO: 435), (SEQ ID NO: 436), (SEQ ID NO: 437), (SEQ ID NO: 438), (SEQ ID NO: 439), (SEQ ID NO: 440), (SEQ ID NO: 441), (SEQ ID NO: 442), (SEQ ID NO: 443), (SEQ ID NO: 444), (SEQ ID NO: 445), (SEQ ID NO: 446), (SEQ ID NO: 447), (SEQ ID NO: 448), (SEQ ID NO: 450), (SEQ ID NO: 451), (SEQ ID NO: 452), (SEQ ID NO: 453), (SEQ ID NO: 454), (SEQ ID NO: 455), (SEQ ID NO: 456), (SEQ ID NO: 457), (SEQ ID NO: 458), (SEQ ID NO: 459), (SEQ ID NO: 460), (SEQ ID NO: 461), (SEQ ID NO: 462), (SEQ ID NO: 463), (SEQ ID NO: 464), (SEQ ID NO: 465), (SEQ ID NO: 466), (SEQ ID NO: 467), (SEQ ID NO: 468), (SEQ ID NO: 469), (SEQ ID NO: 470), (SEQ ID NO: 471), (SEQ ID NO: 472), (SEQ ID NO: 473), (SEQ ID NO: 474), (SEQ ID NO: 475), (SEQ ID NO: 476), (SEQ ID NO: 477), (SEQ ID NO: 478), (SEQ ID NO: 479), (SEQ ID NO: 480), (SEQ ID NO: 481), (SEQ ID NO: 482), (SEQ ID NO: 483), (SEQ ID NO: 484), (SEQ ID NO: 485), (SEQ ID NO: 486), (SEQ ID NO: 487), (SEQ ID NO: 488), (SEQ ID NO: 489), (SEQ ID NO: 490), (SEQ ID NO: 491), (SEQ ID NO: 492), and (SEQ ID NO: 493).

3. The multi-epitope T cell immunogen composition of claim 1, wherein the selected HPV epitopes comprise at least one immunogenic region having an amino acid sequence of (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 519), (SEQ ID NO: 520), (SEQ ID NO: 521), (SEQ ID NO: 522), (SEQ ID NO: 523), (SEQ ID NO: 524), (SEQ ID NO: 525), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543) or variants thereof having at least about 65% to about 99% homology to the immunogenic region, and combinations thereof.

4. The multi-epitope T cell immunogen composition of claim 3, wherein the combinations are selected from: i) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); ii) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO:Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iv) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); v) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vi) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); viii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); ix) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); x) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xii) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xiii) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQAttorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xiv) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xv) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xvi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xvii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xviii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xix) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); and xx) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543).

5. The multi-epitope T cell immunogen composition of claim 1, wherein the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to the selected HPV epitope, are selected from Table 1.Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 6. The multi-epitope T cell immunogen composition of claim 5, wherein the two or more HPV epitopes selected from Table 1 are (SEQ ID NO: 608), (SEQ ID NO: 554), (SEQ ID NO: 609), (SEQ ID NO: 610), (SEQ ID NO: 611), (SEQ ID NO: 612), (SEQ ID NO: 613), (SEQ ID NO: 614), (SEQ ID NO: 615), (SEQ ID NO: 616), (SEQ ID NO: 617), (SEQ ID NO: 618), (SEQ ID NO: 619), (SEQ ID NO: 620), (SEQ ID NO: 619), (SEQ ID NO: 552), (SEQ ID NO: 553), (SEQ ID NO: 555), (SEQ ID NO: 556), (SEQ ID NO: 557), (SEQ ID NO: 558), (SEQ ID NO: 559), (SEQ ID NO: 10), (SEQ ID NO: 561), (SEQ ID NO: 562), (SEQ ID NO: 563), (SEQ ID NO: 564), (SEQ ID NO: 565), (SEQ ID NO: 566), (SEQ ID NO: 567), (SEQ ID NO: 568), (SEQ ID NO: 569), (SEQ ID NO: 570), (SEQ ID NO: 571), (SEQ ID NO: 572), (SEQ ID NO: 573), (SEQ ID NO: 574), (SEQ ID NO: 575), (SEQ ID NO: 576), (SEQ ID NO: 577), (SEQ ID NO: 578), (SEQ ID NO: 579), (SEQ ID NO: 580), (SEQ ID NO: 581), (SEQ ID NO: 582), (SEQ ID NO: 583), (SEQ ID NO: 584), (SEQ ID NO: 585), (SEQ ID NO: 586), (SEQ ID NO: 587), (SEQ ID NO: 588), (SEQ ID NO: 589), (SEQ ID NO: 590), (SEQ ID NO: 591), (SEQ ID NO: 592), (SEQ ID NO: 593), and (SEQ ID NO: 594).

7. The multi-epitope T cell immunogen composition of claim 6, wherein the selected HPV epitopes comprise at least one immunogenic region having an amino acid sequence of (SEQ ID NO: 595), (SEQ ID NO: 596), (SEQ ID NO: 597), (SEQ ID NO: 598), (SEQ ID NO: 599), (SEQ ID NO: 600), (SEQ ID NO: 601), (SEQ ID NO: 581), (SEQ ID NO: 602), (SEQ ID NO: 603), (SEQ ID NO: 577), (SEQ ID NO: 605), (SEQ ID NO: 606), or (SEQ ID NO: 607) or variants thereof having at least about 65% to about 99% homology to the immunogenic region and combinations thereof.

8. A vector comprising a multi-epitope T cell immunogen composition comprising two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to an HPV epitope in FIG.

5.

9. The vector of claim 8, wherein the two or more HPV epitopes selected from FIG.5, or variants thereof having at least about 65% to about 99% homology to the selected HPV epitope, are selected from (SEQ ID NO: 107), (SEQ ID NO: 449), (SEQ ID NO: 1), (SEQ ID NO: 2), (SEQ ID NO: 3), (SEQ ID NO: 4), (SEQ ID NO: 5), (SEQ ID NO: 6), (SEQ ID NO: 7), (SEQ ID NO: 8), (SEQ ID NO: 9), (SEQ ID NO: 10), (SEQ ID NO: 11), (SEQ ID NO: 12), (SEQ ID NO: 13), (SEQ ID NO: 14), (SEQ ID NO: 15), (SEQ ID NO: 16), (SEQ ID NO: 17), (SEQ ID NO: 18), (SEQ ID NO: 19), (SEQ ID NO: 20) (SEQ ID NO: 21), (SEQ ID NO: 22), (SEQ ID NO: 23), (SEQ ID NO: 24), (SEQ ID NO: 25), (SEQ ID NO: 26), (SEQ ID NO: 27), (SEQ ID NO: 28), (SEQ ID NO: 29), (SEQ ID NO: 30), (SEQ ID NO: 31), (SEQ ID NO: 32), (SEQ ID NO: 33), (SEQ ID NO: 34), (SEQ ID NO: 35), (SEQ ID NO: 36), (SEQ ID NO: 37), (SEQ ID NO: 38), (SEQ ID NO: 39), (SEQ ID NO: 40), (SEQ ID NO: 41), (SEQ ID NO: 42), (SEQ ID NO: 43), (SEQ ID NO: 44), (SEQ ID NO: 45), (SEQ ID NO: 46), (SEQ ID NO: 47), (SEQ ID NO: 48), (SEQ ID NO: 49), (SEQ ID NO: 50), (SEQ ID NO: 51), (SEQ ID NO: 52), (SEQ ID NO: 53), (SEQ ID NO: 54), (SEQ ID NO: 55), (SEQ ID NO: 56), (SEQ ID NO: 57), (SEQ ID NO: 58), (SEQ ID NO: 59), (SEQ ID NO: 60), (SEQ ID NO: 61), (SEQ ID NO: 62), (SEQ ID NO: 63), (SEQ ID NO: 64), (SEQ ID NO: 65), (SEQ ID NO: 66), (SEQ ID NO: 67), (SEQ ID NO: 68), (SEQ ID NO: 69), (SEQ ID NO: 70), (SEQ ID NO: 71), (SEQ IDAttorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT NO: 72), (SEQ ID NO: 73), (SEQ ID NO: 74), (SEQ ID NO: 75), (SEQ ID NO: 76), (SEQ ID NO: 77), (SEQ ID NO: 78), (SEQ ID NO: 79), (SEQ ID NO: 80), (SEQ ID NO: 81), (SEQ ID NO: 82), (SEQ ID NO: 83), (SEQ ID NO: 84), (SEQ ID NO: 85), (SEQ ID NO: 86), (SEQ ID NO: 87), (SEQ ID NO: 88), (SEQ ID NO: 89), (SEQ ID NO: 90), (SEQ ID NO: 91), (SEQ ID NO: 92), (SEQ ID NO: 93), (SEQ ID NO: 94), (SEQ ID NO: 95), (SEQ ID NO: 96), (SEQ ID NO: 97), (SEQ ID NO: 98), (SEQ ID NO: 99), (SEQ ID NO: 100), (SEQ ID NO: 101), (SEQ ID NO: 102), (SEQ ID NO: 103), (SEQ ID NO: 104), (SEQ ID NO: 105), (SEQ ID NO: 106), (SEQ ID NO: 108), (SEQ ID NO: 109), (SEQ ID NO: 110), (SEQ ID NO: 111), (SEQ ID NO: 112), (SEQ ID NO: 113), (SEQ ID NO: 114), (SEQ ID NO: 115), (SEQ ID NO: 116) (SEQ ID NO: 116), (SEQ ID NO: 117), (SEQ ID NO: 118), (SEQ ID NO: 119), (SEQ ID NO: 120), (SEQ ID NO: 121), (SEQ ID NO: 122), (SEQ ID NO: 123), (SEQ ID NO: 124), (SEQ ID NO: 125), (SEQ ID NO: 126), (SEQ ID NO: 127), (SEQ ID NO: 128), (SEQ ID NO: 129), (SEQ ID NO: 130), (SEQ ID NO: 131), (SEQ ID NO: 132), (SEQ ID NO: 133), (SEQ ID NO: 134), (SEQ ID NO: 135), (SEQ ID NO: 136), (SEQ ID NO: 137), (SEQ ID NO: 138), (SEQ ID NO: 139), (SEQ ID NO: 140), (SEQ ID NO: 141), (SEQ ID NO: 142) (SEQ ID NO: 143), (SEQ ID NO: 144), (SEQ ID NO: 145), (SEQ ID NO: 146), (SEQ ID NO: 147), (SEQ ID NO: 148), (SEQ ID NO: 149), (SEQ ID NO: 150), (SEQ ID NO: 151), (SEQ ID NO: 152), (SEQ ID NO: 153), (SEQ ID NO: 154), (SEQ ID NO: 155), (SEQ ID NO: 156), (SEQ ID NO: 157), (SEQ ID NO: 158), (SEQ ID NO: 159), (SEQ ID NO: 160), (SEQ ID NO: 161), (SEQ ID NO: 162), (SEQ ID NO: 163), (SEQ ID NO: 164), (SEQ ID NO: 165), (SEQ ID NO: 166), (SEQ ID NO: 167), (SEQ ID NO: 168), (SEQ ID NO: 169), (SEQ ID NO: 170), (SEQ ID NO: 171), (SEQ ID NO: 172), (SEQ ID NO: 173), (SEQ ID NO: 174), (SEQ ID NO: 175), (SEQ ID NO: 176), (SEQ ID NO: 177), (SEQ ID NO: 178), (SEQ ID NO: 179), (SEQ ID NO: 180), (SEQ ID NO: 181), (SEQ ID NO: 182), (SEQ ID NO: 183), (SEQ ID NO: 184), (SEQ ID NO: 185), (SEQ ID NO: 186), (SEQ ID NO: 187), (SEQ ID NO: 188), (SEQ ID NO: 189), (SEQ ID NO: 190), (SEQ ID NO: 191), (SEQ ID NO: 192), (SEQ ID NO: 193), (SEQ ID NO: 194), (SEQ ID NO: 195), (SEQ ID NO: 196), (SEQ ID NO: 197), (SEQ ID NO: 198), (SEQ ID NO: 199), (SEQ ID NO: 200), (SEQ ID NO: 201), (SEQ ID NO: 202), (SEQ ID NO: 203), (SEQ ID NO: 204), (SEQ ID NO: 205), (SEQ ID NO: 206), (SEQ ID NO: 207), (SEQ ID NO: 208), (SEQ ID NO: 209), (SEQ ID NO: 210), (SEQ ID NO: 211), (SEQ ID NO: 212), (SEQ ID NO: 213), (SEQ ID NO: 214), (SEQ ID NO: 215), (SEQ ID NO: 216), (SEQ ID NO: 217), (SEQ ID NO: 218), (SEQ ID NO: 219), (SEQ ID NO: 220), (SEQ ID NO: 221), (SEQ ID NO: 222), (SEQ ID NO: 223), (SEQ ID NO: 224), (SEQ ID NO: 225), (SEQ ID NO: 226), (SEQ ID NO: 227), (SEQ ID NO: 228), (SEQ ID NO: 229), (SEQ ID NO: 230), (SEQ ID NO: 231), (SEQ ID NO: 232), (SEQ ID NO: 233), (SEQ ID NO: 234), (SEQ ID NO: 235), (SEQ ID NO: 236), (SEQ ID NO: 237), (SEQ ID NO: 238), (SEQ ID NO: 239), (SEQ ID NO: 240), (SEQ ID NO: 241), (SEQ ID NO: 242), (SEQ ID NO: 243), (SEQ ID NO: 244), (SEQ ID NO: 245), (SEQ ID NO: 246), (SEQ ID NO: 247), (SEQ ID NO: 248), (SEQ ID NO: 249), (SEQ ID NO: 250), (SEQ ID NO: 251), (SEQ ID NO: 252), (SEQ ID NO: 253), (SEQ ID NO: 254), (SEQ ID NO: 255), (SEQ ID NO: 256), (SEQ ID NO: 257), (SEQ ID NO: 258), (SEQ ID NO: 259), (SEQ ID NO: 260), (SEQ ID NO: 261), (SEQ ID NO: 262), (SEQ ID NO: 263), (SEQ ID NO: 264), (SEQ ID NO: 265), (SEQ ID NO: 266), (SEQ ID NO: 267), (SEQ ID NO: 268), (SEQ ID NO: 269), (SEQ ID NO: 270), (SEQ ID NO: 271), (SEQ ID NO: 272), (SEQ ID NO: 273), (SEQ ID NO: 274), (SEQ ID NO: 275), (SEQ ID NO: 276), (SEQ ID NO: 277), (SEQ ID NO: 278), (SEQ ID NO: 279), (SEQ ID NO: 280), (SEQ ID NO: 281), (SEQ ID NO: 282), (SEQ ID NO: 283), (SEQ ID NO: 284), (SEQ ID NO: 285), (SEQ ID NO: 286), (SEQ ID NO: 287), (SEQ ID NO: 288), (SEQ ID NO: 289), (SEQ ID NO: 290), (SEQ ID NO: 291), (SEQ ID NO:Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 292), (SEQ ID NO: 293), (SEQ ID NO: 294), (SEQ ID NO: 295), (SEQ ID NO: 296), (SEQ ID NO: 297), (SEQ ID NO: 298), (SEQ ID NO: 299), (SEQ ID NO: 300), (SEQ ID NO: 301), (SEQ ID NO: 302), (SEQ ID NO: 303), (SEQ ID NO: 304), (SEQ ID NO: 305), (SEQ ID NO: 306), (SEQ ID NO: 307), (SEQ ID NO: 308), (SEQ ID NO: 309), (SEQ ID NO: 310), (SEQ ID NO: 311), (SEQ ID NO: 312), (SEQ ID NO: 313), (SEQ ID NO: 314), (SEQ ID NO: 315), (SEQ ID NO: 316), (SEQ ID NO: 317), (SEQ ID NO: 318), (SEQ ID NO: 319), (SEQ ID NO: 320), (SEQ ID NO: 321), (SEQ ID NO: 322), (SEQ ID NO: 323), (SEQ ID NO: 324), (SEQ ID NO: 325), (SEQ ID NO: 326), (SEQ ID NO: 327), (SEQ ID NO: 328), (SEQ ID NO: 329), (SEQ ID NO: 330), (SEQ ID NO: 331), (SEQ ID NO: 332), (SEQ ID NO: 333), (SEQ ID NO: 334), (SEQ ID NO: 335), (SEQ ID NO: 336), (SEQ ID NO: 337), (SEQ ID NO: 338), (SEQ ID NO: 339), (SEQ ID NO: 340), (SEQ ID NO: 341), (SEQ ID NO: 342), (SEQ ID NO: 343), (SEQ ID NO: 344), (SEQ ID NO: 345), (SEQ ID NO: 346), (SEQ ID NO: 347), (SEQ ID NO: 348), (SEQ ID NO: 349), (SEQ ID NO: 350), (SEQ ID NO: 351), (SEQ ID NO: 352), (SEQ ID NO: 353), (SEQ ID NO: 354), (SEQ ID NO: 355), (SEQ ID NO: 356), (SEQ ID NO: 357), (SEQ ID NO: 358), (SEQ ID NO: 359), (SEQ ID NO: 360), (SEQ ID NO: 361), (SEQ ID NO: 362), (SEQ ID NO: 363), (SEQ ID NO: 364), (SEQ ID NO: 365), (SEQ ID NO: 366), (SEQ ID NO: 367), (SEQ ID NO: 368), (SEQ ID NO: 369), (SEQ ID NO: 370), (SEQ ID NO: 371), (SEQ ID NO: 372), (SEQ ID NO: 373), (SEQ ID NO: 374), (SEQ ID NO: 375), (SEQ ID NO: 376), (SEQ ID NO: 377), (SEQ ID NO: 378), (SEQ ID NO: 379), (SEQ ID NO: 380), (SEQ ID NO: 381), (SEQ ID NO: 382), (SEQ ID NO: 383), (SEQ ID NO: 384), (SEQ ID NO: 385), (SEQ ID NO: 386), (SEQ ID NO: 387), (SEQ ID NO: 388), (SEQ ID NO: 389), (SEQ ID NO: 390), (SEQ ID NO: 391), (SEQ ID NO: 392), (SEQ ID NO: 393), (SEQ ID NO: 394), (SEQ ID NO: 395), (SEQ ID NO: 396), (SEQ ID NO: 397), (SEQ ID NO: 398), (SEQ ID NO: 399), (SEQ ID NO: 400), (SEQ ID NO: 401), (SEQ ID NO: 402), (SEQ ID NO: 403), (SEQ ID NO: 404), (SEQ ID NO: 405), (SEQ ID NO: 406), (SEQ ID NO: 407), (SEQ ID NO: 408), (SEQ ID NO: 409), (SEQ ID NO: 410), (SEQ ID NO: 411), (SEQ ID NO: 412), (SEQ ID NO: 413), (SEQ ID NO: 414), (SEQ ID NO: 415), (SEQ ID NO: 416), (SEQ ID NO: 417), (SEQ ID NO: 418), (SEQ ID NO: 419), (SEQ ID NO: 420), (SEQ ID NO: 421), (SEQ ID NO: 422), (SEQ ID NO: 423), (SEQ ID NO: 424), (SEQ ID NO: 425), (SEQ ID NO: 426), (SEQ ID NO: 427), (SEQ ID NO: 428), (SEQ ID NO: 429), (SEQ ID NO: 430), (SEQ ID NO: 431), (SEQ ID NO: 432), (SEQ ID NO: 433), (SEQ ID NO: 434), (SEQ ID NO: 435), (SEQ ID NO: 436), (SEQ ID NO: 437), (SEQ ID NO: 438), (SEQ ID NO: 439), (SEQ ID NO: 440), (SEQ ID NO: 441), (SEQ ID NO: 442), (SEQ ID NO: 443), (SEQ ID NO: 444), (SEQ ID NO: 445), (SEQ ID NO: 446), (SEQ ID NO: 447), (SEQ ID NO: 448), (SEQ ID NO: 450), (SEQ ID NO: 451), (SEQ ID NO: 452), (SEQ ID NO: 453), (SEQ ID NO: 454), (SEQ ID NO: 455), (SEQ ID NO: 456), (SEQ ID NO: 457), (SEQ ID NO: 458), (SEQ ID NO: 459), (SEQ ID NO: 460), (SEQ ID NO: 461), (SEQ ID NO: 462), (SEQ ID NO: 463), (SEQ ID NO: 464), (SEQ ID NO: 465), (SEQ ID NO: 466), (SEQ ID NO: 467), (SEQ ID NO: 468), (SEQ ID NO: 469), (SEQ ID NO: 470), (SEQ ID NO: 471), (SEQ ID NO: 472), (SEQ ID NO: 473), (SEQ ID NO: 474), (SEQ ID NO: 475), (SEQ ID NO: 476), (SEQ ID NO: 477), (SEQ ID NO: 478), (SEQ ID NO: 479), (SEQ ID NO: 480), (SEQ ID NO: 481), (SEQ ID NO: 482), (SEQ ID NO: 483), (SEQ ID NO: 484), (SEQ ID NO: 485), (SEQ ID NO: 486), (SEQ ID NO: 487), (SEQ ID NO: 488), (SEQ ID NO: 489), (SEQ ID NO: 490), (SEQ ID NO: 491), (SEQ ID NO: 492), and (SEQ ID NO: 493).

10. The vector of claim 8, wherein the selected HPV epitopes comprise at least one immunogenic region having an amino acid sequence of (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ IDAttorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 519), (SEQ ID NO: 520), (SEQ ID NO: 521), (SEQ ID NO: 522), (SEQ ID NO: 523), (SEQ ID NO: 524), (SEQ ID NO: 525), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543) or variants thereof having at least about 65% to about 99% homology to the immunogenic region, and combinations thereof.

11. The vector of claim 10, wherein the combinations are selected from: i) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); ii) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); iv) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (16E2 F7), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); v) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vi) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); vii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), and (SEQ ID NO: 520); viii) (SEQ ID NO: 495), (SEQ ID NO: 496), (SEQ ID NO: 497), (SEQ ID NO: 498), (SEQ ID NO: 499), (SEQ ID NO: 500), (SEQ ID NO: 501), (SEQ ID NO: 502), (SEQ ID NO: 503), (SEQ ID NO:Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 544), and (SEQ ID NO: 545); ix) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); x) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xii) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xiii) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xiv) (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xv) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xvi) (SEQ ID NO: 522), (SEQ ID NO: 524), (SEQ ID NO: 526), (SEQ ID NO: 527), (SEQ ID NO: 528), (SEQ ID NO: 529), (SEQ ID NO: 530), (SEQ ID NO: 531), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 548), and (SEQ ID NO: 549); xvii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xviii) (SEQ ID NO: 494), (SEQ ID NO: 495), (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 511), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 515), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 519), (SEQ ID NO: 521), (SEQ ID NO: 523), (SEQ ID NO: 525), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO:Attorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); xix) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543); and xx) (SEQ ID NO: 504), (SEQ ID NO: 505), (SEQ ID NO: 506), (SEQ ID NO: 507), (SEQ ID NO: 508), (SEQ ID NO: 509), (SEQ ID NO: 510), (SEQ ID NO: 512), (SEQ ID NO: 513), (SEQ ID NO: 514), (SEQ ID NO: 516), (SEQ ID NO: 517), (SEQ ID NO: 518), (SEQ ID NO: 520), (SEQ ID NO: 532), (SEQ ID NO: 533), (SEQ ID NO: 534), (SEQ ID NO: 535), (SEQ ID NO: 536), (SEQ ID NO: 537), (SEQ ID NO: 538), (SEQ ID NO: 539), (SEQ ID NO: 540), (SEQ ID NO: 541), (SEQ ID NO: 542), and (SEQ ID NO: 543).

12. The vector of claim 8, wherein the selected HPV epitopes have an amino acid sequence of an epitope in Table 1, or variants thereof having at least about 65% to about 99% homology to the amino acid sequence of the selected HPV epitope.

13. The vector of claim 12, wherein the two or more HPV epitopes selected from Table 1, or variants thereof having at least about 65% to about 99% homology to the amino acid sequence of the selected HPV epitope, are (SEQ ID NO: 608), (SEQ ID NO: 554), (SEQ ID NO: 609), (SEQ ID NO: 610), (SEQ ID NO: 611), (SEQ ID NO: 612), (SEQ ID NO: 613), (SEQ ID NO: 614), (SEQ ID NO: 615), (SEQ ID NO: 616), (SEQ ID NO: 617), (SEQ ID NO: 618), (SEQ ID NO: 619), (SEQ ID NO: 620), (SEQ ID NO: 619), (SEQ ID NO: 552), (SEQ ID NO: 553), (SEQ ID NO: 555), (SEQ ID NO: 556), (SEQ ID NO: 557), (SEQ ID NO: 558), (SEQ ID NO: 559), (SEQ ID NO: 10), (SEQ ID NO: 561), (SEQ ID NO: 562), (SEQ ID NO: 563), (SEQ ID NO: 564), (SEQ ID NO: 565), (SEQ ID NO: 566), (SEQ ID NO: 567), (SEQ ID NO: 568), (SEQ ID NO: 569), (SEQ ID NO: 570), (SEQ ID NO: 571), (SEQ ID NO: 572), (SEQ ID NO: 573), (SEQ ID NO: 574), (SEQ ID NO: 575), (SEQ ID NO: 576), (SEQ ID NO: 577), (SEQ ID NO: 578), (SEQ ID NO: 579), (SEQ ID NO: 580), (SEQ ID NO: 581), (SEQ ID NO: 582), (SEQ ID NO: 583), (SEQ ID NO: 584), (SEQ ID NO: 585), (SEQ ID NO: 586), (SEQ ID NO: 587), (SEQ ID NO: 588), (SEQ ID NO: 589), (SEQ ID NO: 590), (SEQ ID NO: 591), (SEQ ID NO: 592), (SEQ ID NO: 593), and (SEQ ID NO: 594).

14. The vector of claim 13, wherein the selected HPV epitopes comprise an immunogenic region having an amino acid sequence of (SEQ ID NO: 595), (SEQ ID NO: 596), (SEQ ID NO: 597), (SEQ ID NO: 598), (SEQ ID NO: 599), (SEQ ID NO: 600), (SEQ ID NO: 601), (SEQ ID NO: 581), (SEQ ID NO: 602), (SEQ ID NO: 603), (SEQ ID NO: 577), (SEQ ID NO: 605), (SEQ ID NO: 606), or (SEQ ID NO: 607) or variants thereof having at least about 65% to about 99% homology to the immunogenic region.

15. The vector of claim 8, wherein the vector comprises an endoplasmic reticulumAttorney Docket No.: 51506-003WO4 MGH Docket No.: MGH 2024-223-03 PATENT insertion signal sequence and / or sequence encoding a pan HLA DR-binding epitope.

16. The vector of claim 8, wherein the vector comprises an enzyme cleavage site sequence.

17. The vector of claim 16, wherein the enzyme cleavage site is a furin cleavage site sequence.

18. The vector of claim 8, wherein the sequences encoding the epitopes are directly linked to each other.

19. The vector of claim 8, wherein the sequences encoding the epitopes are linked by a linker sequence.

20. The vector of claim 19, wherein the linker sequence comprises Alanine and Tyrosine.

21. The vector of claim 19, wherein the linker sequence comprises Glycine and Proline.

22. A pharmaceutical composition comprising any one of the immunogen compositions of claims 1-7, or the vector of any one of claims 8 to 21.

23. A method of preventing or treating an HPV infection in a subject, said method comprising administering any one of the immunogen compositions of claims 1-7, or the vector of any one of claims 8 to 21 to the subject.

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