Novel secretory antigen for diagnosing active babesia microti infection and babesia duncani infection in human and animal

Abstract

To provide a method for detecting Babesia infection in a subject in various aspects and modes.SOLUTION: The method includes the following step of detecting one or more peptides selected from SEQ ID NOs: 1-62 in a biological sample taken from a subject, wherein the detection of one or more of peptides indicates the presence of Babesia infection.SELECTED DRAWING: None

Description

[Technical Field]

[0001] CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority under 35 U.S.C. § 119(e) to U.S. Provisional Patent Application No. 62 / 937,645, filed November 19, 2019, and U.S. Provisional Patent Application No. 62 / 860,662, filed June 12, 2019, all of which are hereby incorporated by reference in their entireties.

[0002] STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT This invention was made with government support under grants AI136118, AI123321, AI138139, and GM110506 awarded by the National Institutes of Health. The government has certain rights in this invention. [Background technology]

[0003] Background of the Invention Human babesiosis is an emerging tick-borne disease endemic to the United States and increasingly reported in other parts of the world, including Asia and Europe. Three species, Babesia microti, B. duncani, and B. divergens, have been shown to cause infection in humans, with B. microti accounting for the majority of reported clinical cases worldwide. In susceptible patients, B. microti infection can cause severe symptoms, including respiratory distress, splenic rupture, and renal failure. Mortality rates associated with babesiosis infection range from 6 to 21%. Furthermore, severe infection and end-organ complications can occur in up to 57% of immunocompromised patients. There is a need in the art for compositions and methods useful for detecting and treating babesiosis. The present disclosure addresses this need. Summary of the Invention

[0004] In some embodiments, the present invention provides methods for detecting a Babesia infection in a subject. In some embodiments, the method comprises detecting the presence of one or more secretory antigens selected from SEQ ID NOs: 1-62 in a biological sample collected from the subject, wherein detecting the presence of one or more of the antigens in the biological sample indicates that the subject has a Babesia infection. In some embodiments, the method comprises detecting one or more secretory antigens selected from SEQ ID NOs: 1-62 in a biological sample collected from the subject, wherein detecting one or more of the antigens indicates the presence of a Babesia infection. In some embodiments, the Babesia infection comprises Babesia microti or Babesia duncani. In some embodiments, the biological sample comprises one or more selected from the group consisting of: a blood sample, a red blood cell sample, a white blood cell sample, a plasma sample, a urine sample, a saliva sample, and / or a combination of one or more thereof. In some embodiments, the one or more antigens further comprise BmGPI12. In some embodiments, the subject is a human. In some embodiments, the subject is a mammal known to carry Babesia parasites. In some embodiments, the one or more antigens are detected by one or more antibody-based techniques selected from the group consisting of: Western blot, immunofluorescence assay, IEM, ELISA, PCR amplification-based immunoassay, and immunoprecipitation.

[0005] In certain aspects, the present invention provides diagnostic tools for identifying or diagnosing babesiosis infection. In certain embodiments, the tool comprises: an assay platform and an immunological agent having specificity for one or more Babesia antigens selected from SEQ ID NOs: 1-62. In some embodiments, the babesiosis infection comprises Babesia microti infection or Babesia dunkani infection. In some embodiments, the assay platform comprises one or more selected from the group consisting of: enzyme-based assays, radioimmunoassays, PCR amplification-based immunoassays, fluorogenic immunoassays, chemiluminescence-based assays, immunoblotting assays, and combinations thereof. In some embodiments, the immunological agent comprises one or more of an antibody or antibody fragment.

[0006] In some aspects, the present invention provides methods for treating, ameliorating, and / or preventing Babesia infection in a subject in need thereof. In some embodiments, the method includes the following steps: obtaining a first sample from the subject at a first timepoint; assaying the sample using a diagnostic tool contemplated herein to detect the presence or absence of infection compared to a reference control; administering one or more therapeutic agents to the subject; obtaining a second sample from the subject at a second timepoint, the second timepoint comprising one or more timepoints after the first timepoint; and assaying the second sample obtained from the subject at one or more second timepoints using a diagnostic tool contemplated herein to detect the presence or absence of infection compared to a reference control. In some embodiments, the sample comprises a blood sample. In some embodiments, the infection comprises a Babesia microti infection or a Babesia duncani infection. In some embodiments, the first timepoint is before administering the therapeutic agent. In some embodiments, the second timepoint comprises a period after administering the therapeutic agent.

[0007] In some embodiments, the present invention provides methods for treating, ameliorating, and / or preventing a Babesia infection in a subject, comprising: detecting the presence of one or more peptides selected from SEQ ID NOs: 1-62 in a biological sample obtained from the subject; and administering at least one antiprotozoal therapeutic agent to the subject. [The present invention 1001] 1. A method for detecting a Babesia infection in a subject, the method comprising: Detecting whether one or more secretor antigens selected from SEQ ID NOs: 1-62 are present in a biological sample obtained from the subject, detecting the presence of one or more of said antigens in a biological sample indicates that the subject has a Babesia infection. [The present invention 1002] 1001. The method of claim 1001, wherein the Babesia infection comprises Babesia microti or Babesia duncani. [The present invention 1003] The biological sample comprises: a blood sample, a red blood cell sample, a white blood cell sample, a plasma sample, a urine sample, a saliva sample, and / or a combination of one or more thereof The method of the present invention 1001, comprising one or more selected from the group consisting of: [The present invention 1004] 1001. The method of claim 1001, wherein the one or more antigens further comprise BmGPI12. [The present invention 1005] 1001. The method of claim 1001, wherein the subject is a human. [The present invention 1006] 1002. The method of claim 1001, wherein the subject is a mammal known to carry the Babesia parasite. [The present invention 1007] The one or more antigens are selected from the following: Western blot, immunofluorescence assay, IEM, ELISA, PCR-based immunoassay, and immunoprecipitation 1001. The method of claim 1001, wherein the antibody is detected by one or more antibody-based techniques selected from the group consisting of: [The present invention 1008] assay platform, and Immunological agents having specificity for one or more Babesia antigens selected from SEQ ID NOs: 1-62 10. A diagnostic tool for identifying or diagnosing babesiosis infection, comprising: [The present invention 1009] The diagnostic tool of the present invention 1008, wherein the babesiosis infection comprises a Babesia microti infection or a Babesia duncani infection. [The present invention 1010] The assay platform includes: Enzyme-based assays, radioimmunoassays, PCR-based immunoassays, fluorogenic immunoassays, chemiluminescence-based assays, immunoblotting assays, and combinations thereof A diagnostic tool according to the present invention 1008, comprising one or more species selected from the group consisting of: [The present invention 1011] The diagnostic tool of the present invention 1008, wherein the immunological agent comprises one or more of an antibody or an antibody fragment. [The present invention 1012] 1. A method of treating, ameliorating, and / or preventing a Babesia infection in a subject in need thereof, comprising the steps of: obtaining a first sample from a subject at a first time point; assaying the sample with the diagnostic tool of the present invention 1008 to detect the presence or absence of infection compared to a comparative reference control; administering one or more therapeutic agents to the subject; obtaining a second sample from the subject at a second timepoint, the second timepoint comprising one or more timepoints after the first timepoint; and Assaying a second sample obtained from the subject at a second time point with the diagnostic tool of the present invention 1008 to detect the presence or absence of infection compared to a comparative reference control. [The present invention 1013] The method of claim 1012, wherein the sample comprises a blood sample. [The present invention 1014] The method of claim 1012, wherein the infection comprises a Babesia microti infection or a Babesia duncani infection. [The present invention 1015] The method of claim 1012, wherein the first time point is before administering the therapeutic agent. [The present invention 1016] The method of claim 1013, wherein the second time point is after administering the therapeutic agent. [The present invention 1017] 1. A method of treating, ameliorating, and / or preventing a Babesia infection in a subject, the method comprising: detecting the presence of one or more peptides selected from SEQ ID NOs: 1-62 in a biological sample obtained from the subject; and administering at least one antiprotozoal treatment to the subject. [Brief explanation of the drawings]

[0008] [Figure 1A]Figures 1A-1B demonstrate that BmGPI12 is secreted into the cytoplasm of erythrocytes and subsequently into the extracellular environment of B. microti-infected erythrocytes. Figure 1A shows immunoblotting analysis using pre-immune (PI) rabbit serum and anti-BmGPI12-immune rabbit serum on the fraction of uninfected erythrocytes (UI) or on the fraction of erythrocytes infected with the LabS1 strain of B. microti. S: mouse plasma fraction, recovered after saponin treatment of erythrocytes; H: hemolyzed blood fraction; (P) membrane fraction. In uninfected erythrocytes, the P fraction consists primarily of erythrocyte membranes. In B. microti-infected erythrocytes, the P fraction contains both erythrocyte membranes and protein extracts from isolated parasites. The erythrocyte membrane protein TER-119 (52 kDa) was detected using an anti-TER-119 monoclonal antibody only in the P fraction from uninfected erythrocytes and in the P fraction from B. microti-infected erythrocytes. Figure 1B shows an immunofluorescence assay of mouse erythrocytes infected with the LabS1 strain of B. microti. BmGPI12 was labeled with a polyclonal anti-BmGPI12 antibody and was observable in the parasite cytoplasm, the parasite plasma membrane, the erythrocyte cytoplasm, and within individual vesicles (IV) and tubes of vesicles (TOV) (indicated by arrows). A monoclonal antibody against TER-119 was used to label the plasma membrane of infected mouse erythrocytes. DAPI staining was applied to demonstrate the presence of parasites within erythrocytes by labeling the parasite's nuclear DNA. Staining of control uninfected erythrocytes is shown. Scale bar: 3 μm. [Figure 1B] See legend to Figure 1A. [Figure 2A]Figures 2A-2C demonstrate that B. microti develops an interlacement of vesicles (IOV) system in the cytoplasm of infected erythrocytes. Figure 2A shows results demonstrating that Giemsa-stained blood smears from B. microti-infected erythrocytes revealed tubular structures within the erythrocyte cytoplasm (see arrows), along with a representative image of an erythrocyte infected with LabS1. Scale bar: 3 μm. Figures 2B and 2C show analysis of blood smears from four infected mice over a 13-day period following infection with the LabS1 strain of B. microti. Figure 2B shows the level of parasitemia in individual mice. A total of 5,000 erythrocytes were analyzed per smear (mean ± SEM). Figure 2C shows the percentage of each morphology detected in blood smears on days 3, 5, 7, 10, and 13 postinfection. A total of 20 images per smear were analyzed on a given day (mean ± SEM). [Figure 2B] See legend to Figure 2A. [Figure 2C] See legend to Figure 2A. [Figure 3A] Figures 3A-3C demonstrate that B. microti develops an IOV system in the cytoplasm of infected erythrocytes. Figure 3A shows that EPON-embedded LabS1-infected erythrocytes revealed the presence of IOVs in the erythrocyte cytoplasm. The IOVs contained electron-dense structures identical to the parasite, indicating that these structures were of parasite origin. Various structures of the parasite and the erythrocyte are indicated by arrows. Figures 3B and 3C show a comparison of ultrathin sections of EPON-embedded infected (Figure 3B) and uninfected (Figure 3C) erythrocytes. IV: individual vesicles; P: parasite; PPM: parasite plasma membrane; R: ribosome; RBCC: erythrocyte cytoplasm; RBCM: erythrocyte membrane; TOV: vesicle tube. [Figure 3B] See legend to Figure 3A. [Figure 3C] See legend to Figure 3A. [Figure 4A]Figures 4A-4D demonstrate that BmGPI12 is localized to the parasite plasma membrane and associated with vesicles and tubules. Figures 4A and 4B show immunoelectron microscopy analysis of mouse erythrocytes infected with B. microti LabS1. Ultrathin sections of infected erythrocytes, high-pressure frozen and embedded in Durcupan resin, were immunolabeled with anti-BmGPI12. IV: individual vesicles, P: parasite, PPM: parasite plasma membrane, RBCC: erythrocyte cytoplasm, RBCM: erythrocyte membrane, TOV: vesicle tubule. Figure 4C shows a schematic diagram illustrating the steps in the ultracentrifugation of plasma samples collected from mice infected with B. microti. Figure 4D shows immunoblot analysis using preimmune (PI) serum and anti-BmGPI12 or anti-TER-119 antibodies on intact plasma (PL) or two fractions of plasma (supernatant: Us, and pellet: Up) after ultracentrifugation at 120,000 x g collected from mice infected with B. microti LabS1. Figures 4E–4F show immunoelectron microscopy analysis using anti-BmGPI12 antibody conjugated with 10 nm gold particles on plasma membrane fractions (Up) from mice infected with B. microti LabS1. [Figure 4B] See legend to Figure 4A. [Figure 4C] See legend to Figure 4A. [Figure 4D] See legend to Figure 4A. [Figure 4E] See legend to Figure 4A. [Figure 4F] See legend to Figure 4A. [Figure 5A]Figures 5A–5E show the secretion of the BmIPA48 antigen via vesicles by B. microti. Figure 5A shows the distribution of BmIPA48 in the plasma fraction (S), hemolyzed blood fraction (H), and membrane fraction (P) isolated from uninfected or B. microti (LabS1)-infected erythrocytes by Western blotting using a polyclonal antibody against BmIPA48 (48 kDa). Pre-immune (PI) serum was used as a control. Figure 5B shows immunoblot analysis using pre-immune serum and anti-BmIPA48 serum in either intact plasma (PL) or two fractions (supernatant: Us, and pellet: Up) of plasma collected from mice infected with the LabS1 strain of B. microti. BmIPA48 is primarily associated with plasma membrane fractions. Figure 5C shows an immunofluorescence assay of BmIPA48 distribution in LabS1-infected erythrocytes. BmIPA48 was labeled with a polyclonal antibody and was detectable within the parasite and in separate IVs within the cytoplasm of infected erythrocytes. A monoclonal antibody against TER-119 was applied to label the erythrocyte plasma membrane, and DAPI labeling confirmed the presence of parasite DNA in otherwise enucleated host erythrocytes. Staining of control, uninfected erythrocytes is shown. Figures 5D and 5E show representative images of immunoelectron micrographs of mouse erythrocytes infected with B. microti LabS1. Ultrathin sections of infected erythrocytes, high-pressure frozen and embedded in Durcupan resin, were immunolabeled with anti-BmIPA48 antibody conjugated to 10 nm gold particles. IV: individual vesicles, P: parasite, PPM: parasite plasma membrane, RBCC: erythrocyte cytoplasm, RBCM: erythrocyte membrane, TOV: vesicle tube. [Figure 5B] See legend to Figure 5A. [Figure 5C] See legend to Figure 5A. [Figure 5D] See legend to Figure 5A. [Figure 5E] See legend to Figure 5A. [Figure 6] 6A-6B show a model of vesicle-mediated antigen transport by B. microti. [Figure 7] Figure 7 shows the distribution of BmGPI12 in plasma and erythrocytes infected with the PRA99 strain of B. microti. Immunoblotting analysis was performed using pre-immune (PI) and anti-BmGPI12 polyclonal antibodies in the uninfected erythrocyte fraction (UI) or the erythrocyte fraction infected with the PRA99 strain of B. microti. S: Mouse plasma fraction, recovered after saponin treatment of erythrocytes; H: Hemolyzed blood fraction; (P) Membrane fraction. In uninfected erythrocytes, the P fraction consists primarily of erythrocyte membranes. In B. microti-infected erythrocytes, the P fraction contains both erythrocyte membranes and protein extracts from isolated parasites. The erythrocyte membrane protein TER-119 (52 kDa) was detected using anti-TER-119 monoclonal antibody only in the P fraction from uninfected erythrocytes and in the P fraction from B. microti -infected erythrocytes. [Figure 8] Figure 8 shows the distribution of the apical protein BmRON2 in B. microti-infected cells. (A) Immunoblotting analysis using pre-immune (PI) and anti-BmRON2 polyclonal antibodies in uninfected erythrocyte fractions (UI) or erythrocyte fractions infected with the LabS1 strain of B. microti. S: mouse plasma fraction, recovered after saponin treatment of erythrocytes; H: hemolyzed blood fraction; (P) membrane fraction. Consistent with previous studies, BmRON2 (163 kDa) undergoes proteolysis in infected cells. A 163 kDa band was found in both the P and S fractions, but not in the H fraction, consistent with the presence of BmRON2 on the surface of daughter parasites and its release into plasma after rupture of infected erythrocytes. No signal was detected when pre-immune (PI) rabbit serum was used for immunodetection. [Figure 9A]Figures 9A-9C show electron microscopy evidence for the IOV system emerging from the parasite plasma membrane. Ultrathin EPON sections of B. microti-infected mouse erythrocytes from LabS1 show individual vesicles (Figure 9A) and vesicular tubules emerging from the parasite (Figures 9B and 9C). IV: individual vesicles, P: parasite, PPM: parasite plasma membrane, RBCC: erythrocyte cytoplasm, RBCM: erythrocyte membrane, TOV: vesicular tubules. [Figure 9B] See legend to Figure 9A. [Figure 9C] See legend to Figure 9A. [Figure 10A] Figures 10A-10B show Western blot and immunofluorescence analyses of samples infected with B. dunkanii and analyzed with an antibody against BdGPI2. Figure 10A shows results from a preliminary immunoblot assay using an anti-BdGPI2 peptide antibody (raised in rabbits) in plasma (PL) from uninfected mice (U) or mice infected with B. dunkanii (I), in vivo, or in supernatant fractions (Sup) or parasite fractions (P) from B. dunkanii cultured in vitro on human erythrocytes (I), or from control uninfected human erythrocytes (U). Figure 10B shows fluorescence microscopy imaging of uninfected or B. dunkanii-infected human erythrocytes using an anti-BdGPI2 antibody. A monoclonal antibody against human Band 3 is used as a control to stain the surface of human erythrocytes. DAPI is used to stain the nuclei of the parasites. [Figure 10B] See legend to Figure 10A. [Figure 11A]Figures 11A-11B show Western blot and immunofluorescence analyses of B. dunkani-infected samples analyzed with an antibody against BdMGF3-1 / HSP-70 precursor. Figure 11A shows a preliminary immunoblot assay using an anti-BdHsp70-2 peptide antibody (raised in rabbits) in plasma (PL) from uninfected mice (U) or B. dunkani-infected mice (I), or in supernatant fractions (Sup) or parasite fractions (P) from B. dunkani cultured in vitro on human erythrocytes (I), or from control uninfected human erythrocytes (U). Figure 11B shows fluorescence microscopy analysis using an anti-BdHsp70-2 antibody on uninfected or B. dunkani-infected human erythrocytes. A monoclonal antibody against human Band 3 is used as a control to stain the surface of human erythrocytes. DAPI is used to stain the nuclei of the parasites. [Figure 11B] See legend to Figure 11A. DETAILED DESCRIPTION OF THE INVENTION

[0009] Detailed Description definition Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, the preferred methods and materials are described.

[0010] As used herein, each of the following terms has the meaning associated with it in this section.

[0011] As used herein, the articles "a" and "an" are used 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.

[0012] As used herein, "about," when referring to a measurable value such as an amount, duration, etc., is intended to encompass variations of ±20%, ±10%, ±5%, ±1%, or ±0.1% from the specified value, where such variations are appropriate for practicing the disclosed methods.

[0013] As used herein, "alleviating" a disease, disorder, or condition means reducing the severity of one or more symptoms of the disease, disorder, disorder, or condition.

[0014] The term "antigen," as used herein, is defined as a molecule that provokes an immune response. This immune response may involve either antibody production or activation of specific immunocompetent cells, or both. Those skilled in the art will understand that virtually any macromolecule, including any protein or peptide, can act as an antigen.

[0015] Furthermore, antigens can be derived from recombinant or genomic DNA. Thus, those skilled in the art will understand that any DNA containing a nucleotide sequence or partial nucleotide sequence encoding a protein that elicits an immune response encodes an "antigen," as that term is used herein. Furthermore, those skilled in the art will understand that an antigen need not be encoded solely by the full-length nucleotide sequence of a gene. It is clear that the present invention includes, but is not limited to, the use of partial nucleotide sequences of multiple genes, and that these nucleotide sequences may be arranged in various combinations to elicit a desired immune response. Furthermore, those skilled in the art will understand that an antigen need not be encoded by a "gene" at all. It is clear that an antigen can be synthetically produced or derived from a biological sample. Such biological samples can include, but are not limited to, tissue samples, tumor samples, cells, or biological fluids.

[0016] The term "epitope," as used herein, is defined as a small chemical molecule on an antigen that can elicit an immune response and induce B cell and / or T cell responses. An antigen can have one or more epitopes. Most antigens have multiple epitopes; i.e., they are multivalent. Epitopes generally range in size from about 10 amino acids and / or sugars. Preferably, epitopes are about 4-18 amino acids, more preferably about 5-16 amino acids, even more preferably about 6-14 amino acids, more preferably about 7-12, and most preferably about 8-10 amino acids. Those skilled in the art will understand that, in general, the overall three-dimensional structure of a molecule, rather than its specific linear sequence, is the primary criterion for antigen specificity and thus distinguishes one epitope from another. Based on the present disclosure, a peptide used in the present invention may be an epitope.

[0017] The term "immune response," as used herein, is defined as a cellular response to an antigen that occurs when lymphocytes recognize the antigenic molecule as foreign and induce antibody production and / or activate lymphocytes to eliminate the antigen.

[0018] As used herein, the term "modified" refers to a molecule or cell of the present invention in an altered state or structure. Molecules can be modified in many ways, including chemical, structural, and functional modifications. Cells can be modified by the introduction of nucleic acids.

[0019] As used herein, the term "modulate" refers to a detectable increase or decrease in the level of a response in a subject compared to the level of the response in the subject in the absence of treatment or compound, and / or compared to the level of the response in an otherwise untreated identical subject. The term encompasses disrupting and / or affecting natural signals or responses to produce a beneficial therapeutic response in a subject, preferably a human.

[0020] As used herein, the terms "peptide," "polypeptide," and "protein" are used interchangeably and refer to compounds composed of amino acid residues covalently linked by peptide bonds. A protein or peptide must contain at least two amino acids, and there is no limit to the maximum number of amino acids that can comprise a protein or peptide sequence. A polypeptide includes any peptide or protein containing two or more amino acids linked to each other by peptide bonds. As used herein, the term refers to both short chains, commonly referred to in the art as peptides, oligopeptides, and oligomers, and longer chains, of which many types exist and are commonly referred to in the art as proteins. "Polypeptide" includes, inter alia, biologically active fragments, substantially homologous polypeptides, oligopeptides, homodimers, heterodimers, polypeptide variants, modified polypeptides, derivatives, analogs, and fusion proteins. A polypeptide includes natural peptides, recombinant peptides, synthetic peptides, or combinations thereof.

[0021] As used herein, the term "specifically binds" when used with respect to an antibody refers to an antibody that recognizes a specific antigen but does not substantially recognize or substantially bind to other molecules in a sample. For example, an antibody that specifically binds to an antigen from one species may also bind to antigens from one or more species. However, such interspecies cross-reactivity itself does not change the classification of the antibody as specific. In another example, an antibody that specifically binds to an antigen may also bind to a different allelic form of the antigen. However, such cross-reactivity itself does not change the classification of the antibody as specific. In some examples, the terms "specific binding" or "specifically binds" can be used to refer to the interaction between an antibody, protein, or peptide and a second chemical species, where the interaction is dependent on the presence of a specific structure (e.g., an antigenic determinant or epitope) in the chemical species; for example, an antibody recognizes and binds to a specific protein structure rather than proteins in general. If an antibody is specific for epitope "A," then in a reaction involving labeled "A" and the antibody, the presence of a molecule containing epitope A (or free, unlabeled A) will reduce the amount of labeled A bound to the antibody.

[0022] As used herein, the terms "subject" and "patient" are used interchangeably. As used herein, a subject is preferably a mammal, such as a non-primate (e.g., cows, pigs, horses, cats, dogs, rats, etc.), and a primate (e.g., monkeys and humans), and most preferably a human.

[0023] As used herein, "treat" means to reduce the frequency of symptoms of a disease, disorder, disorder, or adverse condition experienced by a patient.

[0024] The term "therapy" as used herein means treatment and / or prophylaxis. A therapeutic effect is achieved by suppression, amelioration, or eradication of the disease state.

[0025] As used herein, a "therapeutically effective amount" is an amount of a composition of the present invention sufficient to confer a beneficial effect on the individual to whom the composition is administered.

[0026] Ranges: Throughout this disclosure, various aspects of the invention may be expressed in range format. It should be understood that the description in range format is merely for convenience and brevity and is not to be construed as an inflexible limitation on the scope of the invention. Accordingly, the description of a range should be considered to have specifically disclosed all individual numerical values ​​within that range, along with the possible subranges. For example, the description of a range such as 1 to 6 should be considered to have specifically disclosed each individual number within that range, e.g., 1, 2, 2.7, 3, 4, 5, 5.3, and 6, along with subranges such as 1 to 3, 1 to 4, 1 to 5, 2 to 4, 2 to 6, 3 to 6, etc. This applies regardless of the breadth of the range.

[0027] explanation The present invention relates to compositions and methods for detecting, diagnosing, screening, treating, and / or reducing a Babesia infection, such as babesiosis, in a subject. The Babesia infection may include a Babesia microti (B. microti) infection, a Babesia dunkani (B. dunkani) infection, and / or a combination thereof. The subject may include a mammal. In some embodiments, the subject is a human.

[0028] Compositions and methods for detecting and / or diagnosing infections - Patent Application 20070122999 In some embodiments, the present invention provides compositions and methods for detecting an infection in a subject. Infections include parasitic infections, such as Babesia infections caused by one or more Babesia strains. Babesia infections can include Babesia microti (B. microti) infections, Babesia dunkani (B. dunkani) infections, and / or combinations thereof.

[0029] In some embodiments, the composition comprises one or more compositions for detecting one or more secreted antigens. The one or more antigens include one or more antigens produced by one or more cells infected with a Babesia infection (e.g., a B. dunkani infection, a B. microti infection, and / or a combination thereof). The one or more antigens may include one or more peptides, including one or more of SEQ ID NOs: 1-62.

[0030] Compositions for detecting / diagnosing Babesia infections In one aspect, the present invention provides a composition for detecting and / or diagnosing infection in a subject. The composition may include one or more immunological agents for detecting one or more antigens or peptides produced by one or more cells. The one or more antigens or peptides may be detected in a sample obtained from a subject with an infection.

[0031] In various embodiments, the one or more immunological agents include one or more immunological agents specific for one or more antigens produced by one or more types of cells. For example, the one or more immunological agents may include one or more of an antibody, an antibody fragment, an antisense peptide, a synthetic peptide, a synthetic antibody, a synthetic antibody fragment, a synthetic hybridized antibody, or an antibody fragment. The one or more immunological agents detect, bind to, or interact with one or more peptides or antigens produced by one or more types of cells infected with one or more of B. duncani, B. microti, or both. The one or more peptides of the antigen may include one or more selected from SEQ. ID. NOs: 1-46, 47-62. In some embodiments, one or more antigens or peptides selected from SEQ. ID. NOs: 1-46 can be used to detect B. dunkani infection in a sample obtained from a subject. In some embodiments, one or more antigens or peptides selected from SEQ. ID. NOs: 47-62 can be used to detect B. microti infection in a sample obtained from a subject.

[0032] In certain embodiments, the biological sample comprises one or more of blood, urine, saliva, stool, lymph, bile, etc., and / or a combination of one or more thereof. The sample may comprise one or more of a whole blood sample, a plasma sample, a serum sample, a hemolyzed blood sample, etc. In some embodiments, the one or more infected cells comprise one or more cells derived from blood, such as, for example, one or more of red blood cells, white blood cells, plasma cells, platelets, etc.

[0033] Methods for detecting / diagnosing Babesia infections In certain embodiments, the present invention relates to methods for detecting and / or diagnosing one or more Babesia infections, including babesiosis, B. dunkani infection, B. microti infection, and / or combinations thereof.

[0034] In some embodiments, the method includes obtaining one or more biological samples from a subject. The one or more biological samples may include one or more of blood, urine, saliva, stool, lymph, bile, etc., and / or a combination of one or more thereof. Blood samples may include whole blood samples, plasma samples, serum samples, hemolyzed blood samples, etc. The subject may include a human subject. The subject may have a known or suspected infection with one or more Babesia strains, including one or more of B. duncani, B. microti, and / or a combination thereof.

[0035] Embodiments of the method include detecting one or more infections in one or more biological samples obtained from a subject. The one or more infections include one or more of babesiosis, B. duncani infection, B. microti infection, and / or combinations thereof. The infections can be detected using one or more immunological agents specific for one or more antigens or peptides, including one or more of SEQ. ID. NOs: 1-46, 47-62, and / or combinations thereof. In certain embodiments, the one or more antigens or peptides are detected using one or more assay platforms, including, for example, enzyme-based assays, radioimmunoassays, PCR amplification-based assays, fluorogenic immunoassays, chemiluminescence-based assays, immunoblotting assays, and combinations thereof. The assays can include one or more of Western blots, immunofluorescence, immunoelectron microscopy, ELISA, immunoprecipitation, etc.

[0036] In some embodiments, one or more antigens or peptides are detected relative to a reference control. In some embodiments, infection is detected when the signal is greater than or less than a threshold value, a difference compared to a reference control, etc.

[0037] Embodiments of the method include measuring one or more biological samples obtained from a subject to detect the presence of an infection. Embodiments of the method include measuring one or more biological samples obtained from a subject to evaluate the effectiveness of one or more therapeutic agents. In various embodiments, the sample is one or more samples including a blood sample, a serum sample, and / or other suitable one or more bodily fluids. In various embodiments, the subject is a healthy subject, a subject with a confirmed infection, a subject suspected of having an infection, a subject who has been treated for an infection and is believed to no longer be infected, etc. The subject can be evaluated by assaying one or more samples obtained from the subject. One or more samples are evaluated at one or more time points to evaluate the status of the infection and / or the effectiveness of one or more treatments for the infection. In various embodiments, the one or more time points include prior to intended infection, such as about 24 hours prior to infection, between about 24 hours and about 12 hours prior to infection, between about 12 hours and about 8 hours prior to infection, between about 8 hours and about 4 hours prior to infection, between about 4 hours and about 1 hour prior to infection, less than about 1 hour prior to infection, and any and all intervals and increments therebetween, etc. The one or more time points include: at the time of infection, up to 1 hour post-infection, between about 1 hour post-infection and about 1 day post-infection, between about 1 day post-infection and about 2 days post-infection, between about 2 days post-infection and about 3 days post-infection, between about 3 days post-infection and about 4 days post-infection, between about 4 days post-infection and about 5 days post-infection, between about 5 days post-infection and about 6 days post-infection, between about 6 days post-infection and about 7 days post-infection, between about 1 week post-infection and about 2 weeks post-infection, between about 2 weeks post-infection and about 4 weeks post-infection, between about 4 weeks post-infection and about 6 weeks post-infection, etc. In various embodiments, the one or more time points include one or more of the following: at the time of infection, immediately prior to administering the therapeutic agent, at the time of administering the therapeutic agent, and after administering the therapeutic agent. The one or more time points may include: up to 24 hours before administering the therapeutic agent, from about 24 hours to about 12 hours before administering the therapeutic agent, from about 12 hours to about 8 hours before administering the therapeutic agent, from about 8 hours to about 4 hours before administering the therapeutic agent, from about 4 hours to about 1 hour before administering the therapeutic agent, less than about 1 hour before administering the therapeutic agent, and any and all increments and intervals therebetween.In various embodiments, the one or more time points include: up to 1 hour after administration, about 1 hour to about 12 hours after administration, about 12 hours to about 24 hours after administration, about 1 day to about 2 days after administration, about 2 days to about 5 days after administration, about 5 days to about 7 days after administration, about 7 days to about 14 days after administration, about 14 days to about 28 days after administration, about 28 days to about 42 days after administration, etc. The one or more time points can include: about 1 week to about 2 weeks after administration, about 2 weeks to about 4 weeks after administration, about 4 weeks to about 6 weeks after administration, etc.

[0038] The method includes detecting an infection in a subject using one or more techniques as described herein. The method includes administering to the subject an effective amount of at least one therapeutic agent comprising one or more antiprotozoal therapeutic agents. In various embodiments, the antiprotozoal therapeutic agent comprises one or more antiprotozoal agents known in the art. [Example]

[0039] Experimental Example The present invention is described in further detail by reference to the following experimental examples. These examples are provided for illustrative purposes only and, unless otherwise specified, are not intended to be limiting. Therefore, the present invention should in no way be construed as being limited to the following examples, but rather should be construed to encompass any and all variations that become evident as a result of the teachings provided herein.

[0040] Example 1: The Apicomplexa parasite Babesia microti is the primary causative agent of human babesiosis, a malaria-like disease and potentially fatal tick-borne disease. Unlike its close relative, the causative agent of human malaria, B. microti develops within human and mouse erythrocytes in the absence of parasitophorous vacuoles, and its secreted antigens lack the transport motifs found in malaria secreted antigens. Here, we show that after erythrocyte entry, B. microti undergoes a significant morphological change during the production of interdigitating vesicles (IOVs); the IOV system extends from the parasite plasma membrane into the host erythrocyte cytoplasm.

[0041] method Parasite strains The B. microti isolates used in this study were LabS1 and PRA99. These strains were maintained in rag2- / - knockout (B6.129S6-Rag2tm1Fwa N12) mice and SCID (severe combined immunodeficiency) C.B17 SCID CB-Igh-1b / IcrTac-Prkdcscid mice and CB17 / Icr-Prkdcscid / IcrIcoCrl mice, as previously described. Parasitemia was observed in blood thin layers and in the recombinant protein BmIPA48 (Genebank ID # XP_021338473; EupathDB ID#: BMR1_03g00947), consisting of amino acids 1-302 of BmGPI12. TIFF2025186283000001.tif4128, BmRON2 peptide TIFF2025186283000002.tif3128. Monoclonal anti-mouse TER-119 (INVITROGEN®) was used as a control.

[0042] Plasma collection and fractionation testing Blood from uninfected animals or from animals infected with B. microti was collected by cardiac puncture and stored in a test tube containing K2EDTA (dipotassium ethylenediaminetetraacetic acid) solution. To isolate plasma, the samples were centrifuged at 1,300 rpm (200 x g) for 20 minutes at room temperature. The plasma, or supernatant, was removed and transferred to a new 1.7 ml microcentrifuge tube. The remaining cell pellet was washed twice with PBS containing 1% saponin, incubated on ice for 30 minutes, and centrifuged at 9,300 x g for 10 minutes at 4°C. The resulting supernatant (hemolyzed blood) was collected, and the remaining pellet fraction (uninfected) or parasite fraction (infected) was washed twice with PBS and centrifuged at 9,300 x g for 10 minutes at 4°C. The plasma fraction (S), hemolyzed blood fraction (H), and pellet fraction (P) were mixed with Laemmli buffer, separated on SDS-PAGE, and analyzed by immunoblotting.

[0043] Isolation of vesicles from plasma IOVs were isolated from the plasma of uninfected mice or from B. microti-infected mice by sequential centrifugation, following a slightly modified protocol for exosome isolation. Briefly, 400 μl of plasma from each animal was diluted with 5 ml of PBS and centrifuged at 500 x g for 30 minutes, followed by centrifugation at 16,000 x g for 45 minutes to remove microvesicles. IOVs were pelleted by ultracentrifugation (UC) at 120,000 x g for 14 hours at 4°C using a SORVALL™ MTX 150 mini-ultracentrifuge equipped with a S52-ST swinging bucket rotor (THERMO FISHER SCIENTIFIC®). The resulting pellet (P1) was collected, and the supernatant was centrifuged again under the same conditions. The resulting pellet fraction (P2) and supernatant fraction (Us) were collected.

[0044] Immunoblot analysis Equal concentrations of plasma fraction (pre-ultracentrifugation), supernatant fraction (Us), and pellet fraction (Up) obtained after UC were analyzed by immunoblotting. To achieve equal concentrations, the supernatant fraction (Us) was concentrated with 20% trichloroacetic acid. The pellet fractions (P1 and P2) were further diluted and combined into a single pellet (Up). All samples were resuspended in Laemmli buffer and loaded onto 10% Mini-PROTEAN® TGX (BIO-RAD LABORATORIES®, Hercules, CA) and transferred to a nitrocellulose membrane. The membrane was blocked in 5% milk and incubated overnight at 4°C with rabbit anti-BmGPI12 serum (1:250 dilution) or preimmune serum (1:250 dilution). The next day, membranes were washed in TBS-T and incubated with ECL horseradish peroxidase (HRP)-conjugated anti-rabbit IgG (1:10,000 dilution) for 1 hour. After further washing, membranes were incubated with ECL western blotting detection reagents (GE HEALTHCARE®, Amersham, UK) and exposed to X-ray film using KODAK® autoradiography. The same method was used for immunoblotting of parasite and erythrocyte membrane fractions (P), erythrocyte cytoplasmic or hemolysate fractions (H), and plasma or supernatant fractions (S). Polyclonal antibodies, including rabbit anti-BmIPA48 (1:100) and rabbit anti-BmRON2 (1:100), and their corresponding preimmune sera, as well as monoclonal anti-mouse TER-119 antibody (1:500), were also analyzed by immunoblotting.

[0045] Immunofluorescence assay (IFA) Rabbit anti-BmGPI12 (BmSA-1) antibody was used to evaluate the localization of BmGPI12 in LabS1 and PRA99 of B. microti. Rabbit anti-BmIPA48 serum was used to evaluate the localization of BmIPA48 in LabS1. Blood smears were prepared by retroorbital blood collection (centrifugation at 1,500 rpm for 2 minutes (MINISPIN PLUS®, EPPENDORF™) followed by deposition onto a 22 mm x 22 mm thin microscope cover glass (12-542-B; FISHERBRAND®) and immediate transfer into a 6-well plate (COSTAR®, CORNING®) placed on a metal plate cooled on ice. The 6-well plate with the blood smears was then stored at 4°C until further processing. To perform IFA, the thin blood smears were removed from 4°C storage and incubated at 37°C (PRECISION® mechanical convection incubator, model 6) in 1% formaldehyde (28908; THERMO SCIENTIFIC®) diluted in PBS (10010-023; GIBCO®). The smears were fixed with LM for 30 minutes, followed by three brief rinses in PBS. The smears were then incubated for 1 hour at 37°C in blocking buffer (5% heat-inactivated fetal bovine serum (16000-044, GIBCO®), 5% normal goat serum (16210-072; GIBCO-BRL®), and 0.1% saponin (10% stock solution in PBS) (S7900-100G; SIGMA®)) and then rinsed once in wash buffer (0.5% fetal bovine serum, 0.5% normal goat serum, 0.05% saponin). To target mouse erythrocyte membranes, FITC anti-mouse TER-119 / erythroid cells; clone: ​​TER-119 (116206; BIOLEGEND® was used at a 1:1,000 dilution. Anti-BmGPI12 antibody or anti-BmIPA48 antibody was used at a 1:1,000 dilution.

[0046] The smears were incubated with gentle shaking (Orbi-Blotter; BENCHMARK®) either overnight at 4°C or for 1 hour at 37°C. The next day, the slides were washed three times for 2 minutes each with wash buffer and incubated with the secondary antibody, goat anti-rabbit IgG (H+L) rhodamine conjugate (31670, Invitrogen) (1:1,000), for 1 hour at 37°C, and then washed three times for 2 minutes each in wash buffer. After three brief rinses in PBS and one brief rinse in ddH2O, coverslips were mounted onto cleaned, sandblasted, one-sided frosted microscope slides (421-004T; THERMO SCIENTIFIC®) using DAPI-added PROLONG™ Gold antifade reagent (P36935; INVITROGEN®, by THERMO FISHER SCIENTIFIC®) and incubated overnight at room temperature in the dark, after which they were examined using a LEICA® TCS SP8 STED 3X microscope (LEICA® Microsystems GmbH; Wetzlar, Germany).

[0047] Imaging with Leica TCS SP8 STED 3X Confocal images were acquired using a LEICA® TCS SP8 STED 3X microscope. An HC PL APO CS2 100X / 1.40 oil immersion objective was used for image acquisition. FITC anti-mouse TER-119 / red blood cells; clone: ​​TER-119 was excited at 488 nm (500 nm to 571 nm, HyD3), rhodamine was excited at 550 nm (569 nm to 650 nm, HyD3), and DAPI was excited at 405 nm (430 nm to 470 nm, HyD1). The pinhole was set to 1 AU. Images were acquired in unidirectional confocal mode at a scan speed of 1,000 Hz (line average 6). The image size was selected to be 38.75 μm x 38.75 μm (1,024 x 1,024 pixels). The PMT transformer was further activated to allow for the acquisition of DIC images.

[0048] Sample preparation for cryosectioning for electron microscopy Sample pellets were fixed in 4% paraformaldehyde (PFA) in PBS for 30 minutes at room temperature, followed by an additional fixation in 4% PFA at 4°C for 1 hour. They were rinsed in PBS and resuspended in 10% gelatin. The cooled blocks were trimmed and placed in 2.3 M sucrose on a rotor overnight at 4°C. They were transferred to aluminum pins and flash-frozen in liquid nitrogen. The frozen blocks were cut in a LEICA® Cryo-EMUC6 UltraCut, and 65-nm-thick sections were taken using the Tokuyasu method (Tokuyasu, 1973), placed on carbon / formvar-coated grids, and floated on dishes in PBS for immunolabeling.

[0049] Immunolabeling of ultrathin sections Samples were processed according to the method described by Slot and Geuze (Slot and Geuze, Nature Protocols. 2007;2(10):2480-2491). Grids were incubated with rabbit anti-BmGPI12 (1:100) or rabbit anti-BmIPA48 (1:100) and their corresponding preimmune antibodies (1:500). 10 nm Protein A gold (Utrecht Medical Center) was used as the secondary antibody. All grids were rinsed in PBS, fixed with 1% glutaraldehyde for 5 min, rinsed again, and transferred to UA / methylcellulose drops, then collected and dried.

[0050] High-pressure freezing and freeze-substitution Epon sectioning and labeling Samples fixed in 4% PFA were frozen at 2000 psi using a LEICA® HMP100. The frozen samples were then freeze-substituted using a LEICA® Freeze AFS unit, starting at -95°C and using acetone containing 1% osmium tetroxide, 1% glutaraldehyde, and 1% water for 10 hours, warming to -20°C for 12 hours, and then warming to 4°C for 2 hours. The samples were rinsed thoroughly with 100% acetone and infiltrated with DURCUPAN™ resin (ELECTRON MICROSCOPY SCIENCES®) and baked at 60°C for 24 hours. The hardened blocks were cut using a LEICA® UltraCut UC7, and 60 nm sections were collected on formvar / carbon-coated nickel grids.

[0051] Immunolabeling of resin sections Grids were placed section-side down on a drop of 1% hydrogen peroxide for 5 minutes, rinsed, and blocked for nonspecific binding with 3% bovine serum albumin in 1% Triton-X-containing PBS for 30 minutes. The grids were incubated overnight with rabbit anti-BmGPI12 or anti-BmIPA48 primary antibody at a 1:100 ratio, rinsed in buffer, and then incubated with 10 nm Protein A Gold (UtrechtUMC) secondary antibody for 30 minutes. The grids were rinsed and fixed with 1% glutaraldehyde for 5 minutes, rinsed thoroughly in distilled water, and counterstained with 2% uranyl acetate and lead citrate. All grids were viewed at 80 kV on an FEI Tencai Biotwin TEM. Images were acquired using a Morada CCD and iTEM (OLYMPUS®) software.

[0052] Image Processing FIJI (imagej.net / Fiji) and MICROSOFT® POWERPOINT® (MICROSCOFT® Corporation) were used to analyze and prepare for publication raw, EM, and fluorescence images of Giemsa smears. The diameter and length of EM structures were determined using the line tool in FIJI. Huygens Professional software (Scientific Volume Imaging) was further used to deconvolve fluorescence images acquired with a LEICA® TCS SP8 STED 3X.

[0053] Selected results The major secretory antigen of B. microti is localized to vesicular structures associated with parasite morphogenesis. The immunodominant BmGPI12 of B. microti is encoded by a member of the bmn multigene family and is one of the parasite's most highly expressed genes during its development within erythrocytes. Consistent with secretion of BmGPI12 from the parasite into the erythrocyte cytoplasm and subsequent secretion into the host environment, immunoblot analysis using anti-BmGPI12 antibodies on blood collected from mice and fractionated to recover the plasma fraction (S), erythrocyte cytoplasmic fraction (H), and membrane fraction (P) showed that BmGPI12 was present in all three fractions from animals infected with B. microti strains (LabS1 (Figure 1) or PRA99 (Figure 7)), but not from uninfected animals (Figures 1A and 7). As a control, immunoblot analysis performed with a monoclonal antibody against the mouse erythrocyte membrane protein TER-119 (glycophorin A-binding protein (Ly-76)) identified this protein in the membrane fraction (P) of both uninfected and B. microti -infected erythrocytes (Kina et al., 2000, Br J Haematol. 109:280-287), but not in the plasma fraction or cytoplasmic fraction of erythrocytes (Figure 1B). As expected, antibodies against the B. microti rhoptry neck protein BmRON2 identified the protein in membrane and plasma fractions, but not in the cytoplasm of erythrocytes (Figure 8). This protein is highly conserved among Apicomplexan parasites and is localized at the apical end of the parasite (Ord et al., 2016, Infect Immun. 84:1574-1584). This finding is consistent with the association of BmRON2 with the parasite during intraerythrocyte development and its release after rupture of the infected erythrocyte and the escape of the daughter parasites (Ord et al., 2016, Infect Immun. 84:1574-1584).As a control, preimmune serum was used to analyze fractions from uninfected erythrocytes and fractions from erythrocytes infected with B. microti, and no signal could be detected (Fig. 7 and 8).

[0054] The localization of BmGPI12 was further examined by confocal microscopy. Analysis identified BmGPI12 in both the cytoplasm and plasma membrane of parasites, in distinct dendritic structures and distinct foci, and also in the cytoplasm of infected erythrocytes (Figure 1B). These structures are reminiscent of membrane extensions frequently observed at different stages of parasite development in Giemsa-stained blood smears of B. microti-infected erythrocytes (representative images from LabS1) (Figure 2A). Blood smears prepared from four B. microti-infected mice showed that the parasites undergo significant morphological changes throughout their intraerythrocyte life cycle, including ring-like morphology, rings with dendritic tubular vesicular structures (TOVs), dividing parasites (tetrads), and tetrads with TOVs (Figures 2B and 2C). The proportion of parasites with TOV structures was similar to the increasing parasite burden in infected animals, suggesting that the morphogenetic event is part of the intraerythrocytic life cycle of B. microti ( Fig. 2C ).

[0055] Vesicle-mediated transport of BmGPI12 antigen into the cytoplasm of B. microti erythrocytes and into host plasma To investigate the nature of TOV at the ultrastructural level, electron microscopy analyses of ultrathin sections of erythrocytes from mice infected with B. microti were performed. These analyses revealed connected vesicular tubes and individual vesicles in the cytoplasm of infected cells (Figures 3A and 3B and 9), but not in uninfected cells (Figure 3C). The measured diameter of individual vesicles (IV) was approximately 0.110 μm ± 0.0052 μm (mean ± SEM), while the length of the vesicular tubes (TOV) varied between sections, ranging from approximately 0.405 μm ± 0.056 μm (mean ± SEM) to 0.900 μm. Interestingly, detailed analysis of these structures revealed that TOV emerges directly from the parasite plasma membrane and spreads into infected erythrocytes (Figure 3B and Figure 9 (panels B and C)). Both the parasite cytoplasm and the contents of the vesicles and tubules had the same electron density (Figures 3A and 3B and Figure 7), further demonstrating the parasitic origin of the structures.

[0056] To determine whether the IV and TOV structures identified by electron microscopy were the same BmGPI12-positive structures detected by confocal microscopy, immunoelectron microscopy (IEM) analysis was performed on B. microti-infected mouse erythrocytes using an anti-BmGPI12 antibody conjugated to 10 nm gold particles. IEM analysis showed that BmGPI12 was localized to the parasite plasma membrane (PPM), as well as to the IV and TOV (Figures 4A and 4B).

[0057] Transport of BmGPI12-containing vesicles from B. microti -infected erythrocytes The discovery that B. microti produces IV and TOV inside infected erythrocytes and that BmGPI12 is bound to these structures led us to further investigate whether this protein is secreted into the host environment via a vesicle-mediated secretion mechanism or as a free antigen. This was achieved by ultracentrifuging plasma samples from B. microti-infected mice at 120,000 x g to separate the fraction containing membrane-bound structures, including vesicles and tubules (Up, ultracentrifuged pellet fraction), from the fraction containing free protein (Us, ultracentrifuged supernatant fraction) (Figure 4C). As shown in Figure 4D, BmGPI12 was found in both the Up and Us fractions, suggesting that the protein is released into the erythrocyte environment as a membrane-bound protein but can also be found as a free protein, presumably due to cleavage of the GPI anchor by plasma enzymes. The host protein TER-119, which is exclusively associated with erythrocyte membranes, was not found in either the Up or Us fractions (Figure 4D), demonstrating that transported proteins were the predominant proteins found in these fractions. Analysis of the membrane fractions by immunoelectron microscopy identified BmGPI12 associated with vesicular and tubular structures similar in size to those observed inside infected erythrocytes (Figures 4E and 4F).

[0058] Evidence for vesicular transport of the immunodominant antigen BmIPA48 in B. microti To determine whether B. microti uses the vesicular system used to secrete BmGPI12 to transport other antigens, we examined the intracellular distribution of another B. microti antigen, BmIPA48, which has previously been shown to elicit strong IgM and IgG responses in infected outbred mice (Silva et al., 2016, Scientific Reports, 6:35284). BmIPA48 encodes a 48-kDa antigen that contains an N-terminal signal peptide but lacks a GPI anchor motif or transmembrane domain (Silva et al., 2016, Scientific Reports, 6:35284). As shown in Figure 5, BmIPA48 is expressed within the parasite, secreted into the cytoplasm of erythrocytes, and then released into the host plasma (Figure 5A). Similar to BmGPI12, confocal microscopy showed the antigen binding to distinct foci in infected erythrocytes (Figure 5C). However, unlike BmGPI12, analysis of the distribution of BmIPA48 after ultracentrifugation showed that the protein was exclusively present in the vesicle-containing fraction (Up fraction) (Figure 5B). Consistent with these findings, immunoelectron microscopy of B. microti-infected erythrocytes demonstrated the presence of BmIPA48 inside both vesicles found in the parasite cytoplasm and vesicles secreted by the parasite into the erythrocyte cytoplasm (Figures 5D and 5E).

[0059] This study reports the first evidence that the human pathogen B. microti utilizes a novel mechanism to transport parasite proteins into host erythrocytes and subsequently into the erythrocyte environment. This system utilizes a parasite-produced, branching, dendritic membrane network of connected vesicles. We show that at least two immunodominant antigens of B. microti, BmGPI12 and BmIPA48, are transported by the parasite via this mechanism.

[0060] A recent study estimated that approximately 398 proteins may be secreted by B. microti during its development within mammalian erythrocytes (Silva et al., 2016, Scientific Reports, 6:35284). Some of these proteins may be transported to the erythrocyte cytoplasm or erythrocyte membrane, where they may function to regulate the host cell cytoskeleton or facilitate nutrient uptake. Others may be further transported into the host plasma to regulate host responses or induce other changes beneficial to the parasite. Both BmGPI12 and BmIPA48 contain N-terminal signal peptides but lack specific motifs, such as the PEXEL motif, which is found in other parasites of the phylum Apicomplexa and is associated with protein secretion into the host (Cornillot et al., 2016, Transfusion, 56:2085-2099; de Koning-Ward et al., 2016, International journal for parasitology; Lanzer et al., 2006, International journal for parasitology. 36:23-36; Marti et al., 2005, J Cell Biology, 171:587-592; Pelle et al., 2015, Cell Microbiology. 17:1618-1639; Sherling and van Ooij, 2016, FEMS microbiology reviews, 40:701-721). Indeed, all predicted secreted proteins of B. microti lack such motifs (Silva et al., 2016, Scientific reports, 6:35284), suggesting that this parasite may have evolved a novel mode of protein transport.Interestingly, in P. falciparum, the PEXEL motif plays a critical role in the transport of parasite proteins through the parasitophorous vacuole that separates the parasite from the erythrocyte cytoplasm. However, unlike P. falciparum, B. microti spends most of its intraerythrocyte development without a parasitophorous vacuole, thus eliminating the need for a translocon to transport proteins into the host cytoplasm. Consistent with this model, genome analysis of B. microti shows a lack of orthologues for most components of the malarial translocon (Cornillot et al., 2012, Transfusion, 56:2085-2099; Silva et al., 2016, Scientific Reports, 6:35284).

[0061] Electron microscopic analysis of ultrathin sections of B. microti-infected erythrocytes showed that the vesicular interlacing consisted of individual vesicles (IVs) and vesicular tubes (TOVs) with diameters of approximately 0.110 μm ± 0.0052 μm. Giemsa staining indicated that the length of the TOVs varied among infected erythrocytes, with some spread of several μm in diameter. Further analysis of blood smears indicated the presence of TOVs throughout the parasite life cycle, and suggested that the production of filamentous forms represents a distinct morphogenetic event in parasite development. Interestingly, analysis of frozen sections showed that the IOV system of B. microti is organized similarly to that of the parasite cytoplasm. A magnified section near the parasite's plasma membrane in Figure 3B showed that a tubule consisting of two vesicles emerged directly from the parasite's plasma membrane. This distinguishes this system from the TVM system previously described in P. falciparum, which has been shown to emerge from the membrane of the parasitophorous vacuole of the malaria parasite.

[0062] This study utilized a fractionation method used to characterize secretory vesicles produced by B. microti. Using this approach, we found that BmGP12 was readily detectable in both the soluble and membrane fractions after centrifugation of plasma samples or the culture medium of short-term cultured parasites, whereas BmIPA48 was found primarily in the vesicle-enriched membrane fraction. The difference in the distribution of these two proteins may be due to their respective localization in vesicles and tubules. Immunoelectron microscopy analysis showed that BmGPI12 was found primarily in the plasma membrane of the parasite and in the membranes of vesicles and tubules. Interestingly, 10 nm gold particles were detectable both inside and outside these vesicles and tubules. Thus, after vesicle release, BmGPI12 exposed on the outside of the vesicles may be cleaved and thus found in the soluble fraction, while proteins still present inside the vesicles may remain associated with the membrane fraction. On the other hand, immunoelectron microscopy analysis of BmIP48 showed that the protein was primarily present inside the vesicles, consistent with its exclusive association with the membrane fraction. Interestingly, no vesicles were detected in the outer layer of the erythrocyte membrane of infected cells, suggesting that vesicles may be released into the host environment after rupture of B. microti-infected erythrocytes, as suggested in our model (Figures 6A-6B).

[0063] Example 2: Secreted antigens of B. microti identified by the NANOTRAP® proteomics approach Table 1. List of 15 transported antigens of B. microti identified using the NANOTRAP® proteomics approach. TIFF2025186283000003.tif104159

[0064] Example 3: Secreted antigens of B. duncani identified by the NANOTRAP® proteomics approach Table 2. List of 46 transported proteins in B. duncani identified by the NANOTRAP®-based proteomics approach. TIFF2025186283000004.tif204151

[0065] Example 4. Secretory antigens of Babesia duncani: SEQ ID NO: 1-46 Table 3: Secreted antigens of B. duncani identified in the pellet fraction after ultracentrifugation of the culture supernatant: SEQ ID NOs: 1-23 TIFF2025186283000005.tif235162TIFF2025186283000006.tif245162TIFF2025186283000007.tif245162TIFF2025186283000008.tif24616 2TIFF2025186283000009.tif245162TIFF2025186283000010.tif246162TIFF2025186283000011.tif245162TIFF2025186283000012.tif64162

[0066] Table 4: Secretory antigens of B. duncani identified in the supernatant fraction: SEQ ID NOs: 24-37 TIFF2025186283000013.tif158168TIFF2025186283000014.tif245168TIFF2025186283000015.tif245168TIFF2025186283 000016.tif244168TIFF2025186283000017.tif245168TIFF2025186283000018.tif245168TIFF2025186283000019.tif69168

[0067] Table 5. Secretory antigens of B. duncani identified in hemolyzed blood fractions: SEQ ID NOs: 38-46 TIFF2025186283000020.tif153168TIFF2025186283000021.tif246168TIFF2025186283000022.tif128168

[0068] Example 5. Secretory antigens of Babesia microti: SEQ ID NO: 47-63 Table 6: Secretory antigens of B. microti identified in the supernatant fraction: SEQ ID NOs: 47-54 TIFF2025186283000023.tif89168TIFF2025186283000024.tif245168TIFF2025186283000025.tif113168

[0069] Table 7: Secretory antigens of B. microti identified in hemolyzed blood fractions: SEQ ID NOs: 55-62 TIFF2025186283000026.tif99168TIFF2025186283000027.tif245168TIFF2025186283000028.tif245168TIFF2025186283000029.tif142168

[0070] equivalent While preferred embodiments of the present invention have been described using specific language, it will be understood that such description is for purposes of illustration only and that modifications and variations may be made without departing from the spirit or scope of the appended claims.

[0071] INCORPORATION BY REFERENCE The entire contents of all patents, published patent applications, and other references cited herein are hereby expressly incorporated herein by reference in their entirety.

[0072] Sequence information SEQUENCE LISTING <110> Yale University <120> NOVEL SECRETED ANTIGENS FOR DIAGNOSIS OF ACTIVE BABESIA MICROTI AND BABESIA DUNCANI INFECTION IN HUMANS AND ANIMALS <150> US 62 / 937,645 <151> 2019-11-19 <150> US 62 / 860,662 <151> 2019-06-12 <160> 62 <170> PatentIn version 3.5 <210> 1 <211> 215 <212> PRT <213> Babesia duncani <400> 1 Met Lys Phe Leu Phe Gly Phe Phe Val Ile Leu Phe Leu Arg Leu Ser 1 5 10 15 Lys Gln Glu Glu Leu Val Ser Leu Gln Leu Gly Asp Phe His Phe Asp 20 25 30 Phe Glu Asn Gly Lys Tyr Ser Thr His Glu Pro Phe Glu Thr Cys Phe 35 40 45 Ile Asp Val Tyr Asn Tyr Arg Tyr Asp Lys Thr Gly Pro Phe Leu Phe 50 55 60 Asn Ile Phe Ile Lys Arg Thr Leu Glu Asn Glu Tyr Gln Ser Leu Phe 65 70 75 80 Phe Lys Arg Glu Asn Gly Lys Leu Val Asn Phe Ala Pro Ser His Leu 85 90 95 Ser Ser Pro Gln Thr Asp Asn Thr Gly Thr Tyr Tyr Ser Thr Lys Glu 100 105 110 Pro Val Val Leu Glu Ser Lys Asn Leu Ser Asp Ile Arg Asn Gly Ile 115 120 125 Lys Lys Ile Gly Gly Asn Lys Leu Ser Ser Ser Gly Lys Ile Asn Trp 130 135 140 Asp Thr Ile Ser Thr Thr Leu Leu Leu Lys Thr Ala Cys Gly Thr Tyr 145 150 155 160 Ser Thr Tyr Ser Ser Gly Tyr Glu Ala Leu Leu Pro Val Lys Asp Gly 165 170 175 Asn Asp Thr Phe Cys Cys Cys Phe Ser Lys Ala Val Leu Phe Thr Gly 180 185 190 Tyr Arg Phe Gln Met Lys Lys Tyr Glu Glu Val Lys Pro Ala Ser Asn 195 200 205 Ser Gln Ser Thr Cys Lys Lys 210 215 <210> 2 <211> 644 <212> PRT <213> babesia duncani <400> 2 Met Ala Ala Thr Ala Ile Gly Ile Asp Leu Gly Thr Thr Tyr Ser Cys 1 5 10 15 Val Ala Val Tyr Lys Asp Asn Asn Val Glu Ile Ile Pro Asn Asp Gln 20 25 30 Gly Asn Arg Thr Thr Pro Ser Tyr Val Ala Phe Thr Asp Thr Glu Arg 35 40 45 Leu Val Gly Asp Ala Ala Lys Asn Gln Glu Ala Arg Asn Pro Glu Asn 50 55 60 Thr Val Phe Asp Val Lys Arg Leu Ile Gly Arg Arg Phe Asp Asp Pro 65 70 75 80 Thr Val Gln Ser Asp Met Lys His Trp Pro Phe Lys Val Asn Ala Gly 85 90 95 Ala Gly Cys Lys Pro Thr Ile Glu Val Thr Phe Glu Gly Gln Lys Lys 100 105 110 Thr Phe His Pro Glu Glu Ile Ser Ser Met Val Leu Ile Lys Met Lys 115 120 125 Glu Ile Ala Glu Ala Tyr Leu Gly Arg Pro Val Thr Asp Ala Val Ile 130 135 140 Thr Val Pro Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ala Thr Lys Asp 145 150 155 160 Ala Gly Thr Ile Ala Gly Leu Asn Val Met Arg Ile Ile Asn Glu Pro 165 170 175 Thr Ala Ala Ala Ile Ala Tyr Gly Leu Asp Lys Lys Gly Ser Thr Glu 180 185 190 Lys Asn Ile Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe Asp Val Ser 195 200 205 Ile Leu Thr Ile Glu Asp Gly Ile Phe Glu Val Lys Ala Thr Thr Gly 210 215 220 Asp Thr His Leu Gly Gly Glu Asp Phe Asp Asn Val Leu Val Glu His 225 230 235 240 Cys Val Arg Asp Phe Met Arg Met Asn Gly Gly Lys Asn Leu Ala Thr 245 250 255 Asn Lys Arg Ala Leu Arg Arg Leu Arg Thr His Cys Glu Arg Ala Lys 260 265 270 Arg Val Leu Ser Ser Ser Thr Gln Ala Thr Ile Glu Leu Asp Ser Leu 275 280 285 Phe Glu Gly Ile Asp Tyr Asn Thr Thr Ile Ser Arg Ala Arg Phe Glu 290 295 300 Glu Met Cys Asn Glu Lys Phe Arg Ser Thr Leu Ile Pro Val Glu Lys 305 310 315 320 Ala Leu Arg Asp Ala Asp Met Asp Lys Arg Lys Ile Asn Glu Val Val 325 330 335 Leu Val Gly Gly Ser Thr Arg Ile Pro Lys Ile Gln Gln Leu Ile Lys 340 345 350 Asp Phe Phe Asn Gly Lys Glu Pro Ser Arg Ser Ile Asn Pro Asp Glu 355 360 365 Ala Val Ala Tyr Gly Ala Ala Val Gln Ala Ala Val Leu Ser Gly Asn 370 375 380 Gln Ser Glu Lys Ile Gln Glu Leu Leu Leu Leu Asp Val Ala Pro Leu 385 390 395 400 Ser Leu Gly Leu Glu Thr Ala Gly Gly Val Met Thr Val Leu Ile Lys 405 410 415 Arg Asn Thr Thr Ile Pro Thr Lys Lys Thr Gln Ile Phe Thr Thr Asn 420 425 430 Glu Asp Arg Gln Glu Gly Val Leu Ile Gln Val Phe Glu Gly Glu Arg 435 440 445 Ala Met Thr Lys Asp Asn Asn Leu Leu Gly Lys Phe His Leu Ser Gly 450 455 460 Ile Ala Pro Ala Pro Arg Gly Val Pro Gln Ile Glu Val Thr Phe Asp 465 470 475 480 Ile Asp Ala Asn Gly Ile Leu Asn Val Thr Ala Met Asp Lys Ser Thr 485 490 495 Gly Lys Ser Glu Gln Val Thr Ile Thr Asn Asp Lys Gly Arg Leu Ser 500 505 510 Gln Thr Asp Ile Asp Arg Met Val Ala Glu Ala Glu Lys Phe Lys Glu 515 520 525 Glu Asp Glu Arg Arg Lys Cys Cys Ile Glu Ser Lys His Lys Leu Glu 530 535 540 Asn Tyr Leu Tyr Ser Met Arg Ser Thr Leu Asn Glu Asp Ala Val Lys 545 550 555 560 Gln Lys Leu Ser Thr Glu Glu Leu Gln Asn Gly Leu Asn Thr Val Glu 565 570 575 Glu Ala Ile Lys Trp Val Glu Asn Asn Gln Leu Ala Asn Gln Asp Glu 580 585 590 Phe Glu Asp Lys Leu Lys Glu Val Glu Lys Ala Cys Ala Pro Leu Thr 595 600 605 Ala Lys Met Tyr Gln Ala Ala Gly Gly Ala Gly Ala Gly Gly Met Pro 610 615 620 Gly Asn Phe Gly Gly Ala Ala Ala Pro Pro Ser Gly Gly Pro Thr Val 625 630 635 640 Glu Glu Val Asp <210> 3 <211> 1058 <212> PRT <213> babesia duncani <400> 3 Met Ala Thr Ile Arg Lys Gln Arg Leu Glu Asp Leu Thr Asp Ile His 1 5 10 15 Lys Glu His Leu Ser Thr Ala His Gln Leu Leu Asp Val Ile Lys Ser 20 25 30 Ala Ser Asp Pro Lys Leu Ile Tyr Leu His Cys Tyr Gln Leu Met Lys 35 40 45 Leu Gly Gly Leu Asp Ala Glu Val Pro Arg Leu Val Val Phe Gly Gln 50 55 60 Gln Ser Met Gly Lys Thr Thr Leu Leu Asp Phe Ile Met Gly Gly Pro 65 70 75 80 Ile Gly Tyr Ser Ser Thr Asp Thr Gly Thr Arg Gln Pro Val Val Ile 85 90 95 Ile Met Arg Pro Glu Ser Ala Ile Asp Pro Arg Glu Leu Glu Leu Ala 100 105 110 Ser Gly Ser Val Gly Ser Pro Ser Ser Thr Ile Thr Ser Lys Lys Ile 115 120 125 Trp Cys Lys Phe Asn Gly Lys Ile Met Asp Ile His Asn Val Gln Gln 130 135 140 Asn Met Arg Leu His Met Gln Ser Leu Gly Glu Arg Ile Cys Ser Glu 145 150 155 160 Glu Leu Glu Val Glu Val Tyr Val Pro Asp Ala Ile Thr Ala Ile Phe 165 170 175 Val Asp Leu Pro Gly Ile Lys Asp Asp Ser Lys Ser Gly Ala Glu Phe 180 185 190 Thr Arg Arg Val Val Arg Asn Tyr Val Ser Asn Asn Pro Asn Asp Leu 195 200 205 Tyr Leu Leu Val Lys Lys Ser Ser Asp Asp Pro Ala Asn Trp Pro Trp 210 215 220 Ser Leu Arg Glu Phe Ile Thr Ala Ala Ala Pro Asn Gly Leu Gly Leu 225 230 235 240 Ser Pro Gln Gln Thr Met Val Val Gly Thr Arg Ala Arg Glu Phe Leu 245 250 255 Ile Asn Glu Lys Thr Asp Ile Arg Thr Gln Asp Gln Leu Tyr Glu Arg 260 265 270 Val His Lys Arg Ala Val Leu Asp Ser Lys Gly Gln Ala Leu Pro Leu 275 280 285 His Leu Leu Glu Leu Phe Ser Leu Ser Ile Gln Ala Lys Asp Lys Gly 290 295 300 Asp Phe Leu Thr Asn Lys Glu Glu Met Lys Arg Gln Ile Ala Asn Gly 305 310 315 320 Gln Val Glu Val Glu Asn Met Ile Arg His Gly Phe Glu Glu Ser Asn 325 330 335 Ser Ile Asn Lys Glu Gly Arg Ser Val Ser Glu Glu Leu Leu Asp Thr 340 345 350 Phe Ser Ile Arg Gln Phe Leu Arg Ser Leu Asn Ser Lys Phe Ser Gln 355 360 365 Leu Leu Asn Gly His Leu Thr Asn Leu Glu Arg Arg Leu Ile Arg Lys 370 375 380 Lys Ile Asp Leu Glu Arg Ile Val Ala Ser Leu Glu Thr Lys Leu Gln 385 390 395 400 Cys Phe Ser Pro Thr Thr Val Arg Glu Ser Ile Lys Gln Phe Ile Arg 405 410 415 Gln Phe Met Glu Ile Val His Asn Met Met Met Gly Asn Tyr Thr Ile 420 425 430 Met Lys Leu Pro Ile Pro Pro Glu Gln Phe Leu Gly Ile Tyr Gly Gly 435 440 445 Ser Leu Arg Asp Asn Leu Glu Asp Gly His Glu Leu Ala Gln Asn Leu 450 455 460 Phe Pro Gln Pro Asp Met Tyr Glu Ser Asn Phe Tyr Thr Lys Ile Thr 465 470 475 480 Ala Arg Thr Glu Glu Leu Tyr Asn Lys Lys Leu Thr Met Ile Asp Thr 485 490 495 Val Lys Pro Gly Arg Tyr Val Arg Tyr Phe Thr Ser Lys Ile Ser Val 500 505 510 His Met Phe Gly Leu Ile Glu Pro Pro Arg Arg Val Pro Pro Ala Val 515 520 525 Ser Gly Ala Asp Leu Gly Pro Phe Asp Met Met Gly Gln Asp Tyr Gly 530 535 540 Ala Asp Glu Leu Ile Asn Val Glu Phe Ile Gln Leu Asn Asn Asn Glu 545 550 555 560 Glu Asn Ser Leu His Lys Asp Ile Asp Arg Ser Lys Leu Ser Leu Leu 565 570 575 Thr Pro Leu Ala Ser Val Ser Ala Glu His Leu Gln Val Pro Leu Tyr 580 585 590 Ala Trp His Lys Thr Lys Glu Pro Lys Thr Gly Trp Val Val Val Arg 595 600 605 Pro Ile Val Ile Asp Arg Leu Pro Pro Glu Ile Leu Val Gln Lys Ser 610 615 620 Asn Tyr Arg Glu Val Asp Val Ala Asn Lys Gln Ile Ser Phe Arg Tyr 625 630 635 640 Leu Asp Val Glu Phe Glu Thr Lys Ala Leu Gly Ser Gly Glu Glu Asp 645 650 655 Gln Leu Glu Asn Ser Val Glu Thr Glu Ile Ser Glu Thr Pro Pro Val 660 665 670 Val Glu Gly Val Gln Asn Arg Cys Ser Asn Arg Tyr Leu Tyr Val Thr 675 680 685 Ala Cys Ser Glu Ile Phe Leu Glu Glu His Arg Thr Ala Pro Tyr Tyr 690 695 700 Ala Ser Ala Leu Glu Met Val Ser Gly Glu His Ala Glu Ala Asn Leu 705 710 715 720 Leu Asn Gln Leu Ala Val Thr Asn Ile Cys His Trp Leu Lys Phe Gln 725 730 735 Ile Lys His Met Glu Pro Glu His Val Tyr Ser Ala Glu Val Leu Tyr 740 745 750 Gln Met Leu Arg Ser Ile Asp His Val Val Asp Arg Ala Asp Trp Glu 755 760 765 Pro Leu Val Ala Asp Leu Val Gln Ser Asn Val Arg Gly Thr Leu Leu 770 775 780 His Ala Ser Arg Leu Ala Ala Cys Ala Ser Ala Ala Ala Leu Arg Arg 785 790 795 800 Val Leu Arg Ala Ser Leu Ala Glu Ala Phe Arg Cys Ile Lys Leu Thr 805 810 815 Asp Cys Asp Gln Thr Leu Tyr Cys Leu Pro Asp Ser Leu His Phe Gln 820 825 830 Glu Gln Ile Asp His Leu Ser Glu Glu Tyr Cys Arg Gln Lys Ala Ile 835 840 845 Asp Cys Ala Asn Ala Met Met Asn Cys Ile Ile Glu Gln Thr Tyr Ser 850 855 860 Ile Gln Phe Asp Val Ala Val Asp Ile Phe Asp Gly Cys Arg Gln Phe 865 870 875 880 Glu Lys Tyr Phe Met Gly Arg Ala Gly His Arg Ser Phe Met Gly Asp 885 890 895 Ala Leu Ser Ser Val Lys Glu Asp Leu Ala Leu Arg Lys Arg Arg Leu 900 905 910 Ala Met Thr Asp Ile Phe Glu Lys Ser Asp Ala Lys Thr Ser Ile Glu 915 920 925 Leu Ile Tyr Glu Glu Val Lys Val Gln Phe Trp Ala Thr Lys Leu Leu 930 935 940 Leu Ser Thr Pro Leu Thr Thr Lys Leu Tyr Thr Tyr Phe Ile Lys Gln 945 950 955 960 Val Val Asp Lys Ala Leu Pro Thr Thr His Ser Asp Pro Thr Ala Ser 965 970 975 Ile Lys Val Glu Phe Glu Gln Phe Leu Ile Asp Asn Ile Leu Tyr Glu 980 985 990 Gln Ile Asp Gly Thr Arg Thr Ala Lys Ser Asn Asn Arg Leu Ser Ala 995 1000 1005 Asp Tyr Asp Leu Asn Asn Lys Tyr Glu Gln Leu Val Gln Gln His 1010 1015 1020 Asn Arg Asn Lys Arg Leu Leu Glu Tyr Ile Ser Cys Ala Leu Glu 1025 1030 1035 Gly Ile Ser Arg Phe Lys His His Ala Thr Ala Asp Thr Asp Phe 1040 1045 1050 Leu Ala His Leu Asp 1055 <210> 4 <211> 2541 <212> PRT <213> babesia duncani <400> 4 Met Ile Ser Ser Pro Pro Ser Gly Phe Ser Leu His Gly Glu Asp Ala 1 5 10 15 Lys Gly Thr Pro Arg Asp Val Glu Arg Gln Asp Ser Asp Arg Leu Asp 20 25 30 Pro Gly Asn Phe Pro Pro Asp Lys Tyr Trp Ser Pro Ser Ile Gly Leu 35 40 45 Ser Thr Ile Glu Ala Asn Arg Arg Val Val Trp Leu Leu Gln Glu Ala 50 55 60 Ile Ser Arg Tyr Lys Ile His Leu Gly Tyr Trp Asn Thr Thr Lys Ser 65 70 75 80 Cys Leu Thr Ile Asp Ile Leu Ile Gly Val Leu Val Leu Val Leu Phe 85 90 95 Ile Leu Gly Ala Glu Pro Asn Leu Gly Val Trp His Val Val Arg Pro 100 105 110 Val Leu Leu Leu Pro Trp Leu Val Leu Asn Cys Tyr Ser Lys Ile Thr 115 120 125 Val Met Arg Ile Lys Ser Ser Arg Ala Cys Glu Arg Val Arg Asp Val 130 135 140 Leu Glu Ser Phe Ser Arg Glu Leu Lys Thr Gly Gly His Thr Glu Val 145 150 155 160 Glu Gln Arg Arg Phe Ser Phe Asp Pro Pro Asn Ser Leu Leu Ile Pro 165 170 175 Val Tyr Arg Asp Arg Glu Trp Lys Arg Leu Pro Ala Asn Val Leu Leu 180 185 190 Ala Gly Asp Val Phe Lys Leu Gln Ile Gly Asp Tyr Phe Pro Cys Asn 195 200 205 Cys Arg Ile Ile Leu Ser Cys Asp Arg Glu Gly Lys Val Gln Leu Asp 210 215 220 Ala Asn Leu Phe Asn Ala Gly Ser Val Phe Lys Ser Ser His Leu Pro 225 230 235 240 Ser Ile Asn Thr Asn Asp Gly Gly Glu Trp Thr Asp Ala Ser Phe Val 245 250 255 Ala Val Thr Asp Ser Phe Val Gln Ser Leu Glu Thr Phe Leu Ser Ala 260 265 270 Asp Gln Gly Pro Gln Ser Arg Phe Met Phe Phe Asn Glu Arg Asp Trp 275 280 285 Glu Asn Cys Gln Lys Gly Pro Asn Thr Pro Pro Pro Thr Thr Cys Val 290 295 300 Trp Asn Phe Ser Asp Tyr Thr His Phe Ser Lys Tyr Gly Val Asp Trp 305 310 315 320 Ile Gln Leu Gly Ile Ala Phe Phe Ile Ser Ser Ile Val Thr Val Leu 325 330 335 Gln Ile Ile Trp Ser Gly Phe Gln Gly Trp Arg Arg His Val Asn Val 340 345 350 Phe Ala Thr Cys Ile Ile Cys Leu Cys His Pro Ala Phe Asp Pro Phe 355 360 365 Leu Asn Leu Ala Asp Ile Trp Gly Asn Val Lys Leu Gln Ser Leu Phe 370 375 380 Gln Trp His Asn Glu Lys Arg Phe Thr Val Asp Ile Leu Pro Gln Gln 385 390 395 400 Ser Ser Ser Ser Ser Ser Thr Phe Asp Ser Gly Ser Ser Glu Asp Ser 405 410 415 Val Asp Ser Glu Met Ala Ala Ser Arg Ile Pro Leu Leu His Gln Leu 420 425 430 Arg Glu Leu Asn Arg Val Phe Lys Arg Gly Leu Asp Ser Glu Gly Ser 435 440 445 Leu Leu Arg Thr Leu Cys Ser Val Thr Leu Leu Cys Phe Val Asp Asp 450 455 460 Met Gly Leu Leu Thr Glu Gly Cys Ala Thr Pro Gln Glu Leu Ala Val 465 470 475 480 Val Asp Pro Ser Gly Gly Ile Gly Thr Gln Arg Arg Gln Gln Lys Glu 485 490 495 Ser Thr Ala Met Phe Gln Ser Gly Asn Ile Asp Ala Ile Glu Thr Ile 500 505 510 Asn Ser Thr Ala Thr Ser His Lys Asp Ser Ile Gly Gln Thr Glu Gln 515 520 525 Ser Asp Lys Gly Thr Ile Lys Ala Gly Pro Arg Glu Gly Lys Gln Val 530 535 540 Val Arg Lys Asp Pro Gln Gly Gly Glu Arg Leu Val Ile Leu Asp Val 545 550 555 560 Phe Glu Asp Ser Ser Gln Tyr Tyr Lys Gln Tyr Val Lys Phe Asn Asn 565 570 575 Asp Ala Glu Arg Asn Cys Ile Pro Gln Val Leu Ser Leu Ser Phe Ala 580 585 590 Met Ser Ala Thr Gln Phe Pro Arg Val Gln Pro Ser Leu Leu Gln Leu 595 600 605 Lys Ala Ala Pro Asp Leu Ile His Thr Tyr Met Gly Met Leu Ala Asn 610 615 620 Gly Thr Leu His Asp Phe Thr His Cys Leu Cys Ala Phe Ala Gly Ser 625 630 635 640 Val Gly Leu Lys Arg Ser Tyr Ile Arg Arg Phe Arg Leu Leu Arg Phe 645 650 655 Ile Val Val Leu Asp Glu Thr Leu Gly Thr Asn Gly Lys Met Leu Ile 660 665 670 Tyr Phe Leu Arg Asp Pro Arg Lys Gln Ile Val Gln Met Leu Val Lys 675 680 685 Ala Lys Pro Glu Thr Val Phe Asp Arg Ser Ile Asn Tyr His Asp Arg 690 695 700 Ala Arg Gly Ala Ile Leu Pro Val Ser Arg Leu Thr Lys Arg Lys Leu 705 710 715 720 Arg Asp Leu Asn Met Gln Trp Val Ser Ser Gly Leu Thr Pro Phe Ala 725 730 735 Phe Ile Tyr Lys Pro Ile His Leu Asp Glu Phe Asn Leu Ile Met Ala 740 745 750 His Leu Pro Gly Val Ala Val Phe Lys Val Gly His Phe Leu Lys Leu 755 760 765 Asp Arg His Gln Ser Val Lys Tyr Gln Glu Ser Thr Thr Cys Gln Gln 770 775 780 Asp Pro Gln Ala Asp Tyr Phe Gly Glu Gly Gly Lys Ser Asp Ala Lys 785 790 795 800 Ala Arg Arg Trp Tyr Ala Arg Leu Thr Asp Tyr Asp Ala Ile Ser Met 805 810 815 Arg Tyr Gly Ser Met His Thr Asp Leu Arg Gln Arg Ile Leu Thr Asn 820 825 830 Ser Ile Gly Gly Leu Val Asn Ser Cys Leu Lys Asn Ser Ile Leu Leu 835 840 845 Gly Met Cys Ala Thr Lys Tyr Gln Tyr Pro Lys Glu Val Pro Ser Arg 850 855 860 Ile Gln Ser Phe His Glu Ala Gly Ile Arg Phe Val Tyr Phe Ser Lys 865 870 875 880 His Asp Glu Lys Gln Thr Arg Ile Val Gly Gly Leu Leu Gly Leu Glu 885 890 895 Thr Ser Trp Asn Ser Met Ile Ser Leu Val Lys Ser Gly Arg Tyr Ser 900 905 910 His Val Asn Gln Asp Gly Arg Val Val Leu Pro Ser Gly Ile Asp Asn 915 920 925 Ile Arg Arg His Ile Arg Asp Val Asp Asp Ile Pro Leu Gln Val Ser 930 935 940 Leu Phe Cys Asp Cys Thr His Thr Ser Thr Val Glu Met Met Arg Ile 945 950 955 960 Leu Arg Glu Asn Gly Glu Arg Ile Met Cys Val Gly Asn Gly Leu Arg 965 970 975 Pro Ser Asn Phe Phe Val Phe Cys Glu Ala His Ser Ser Val Ser Val 980 985 990 Ala Leu Gly Tyr His Pro Thr Cys Arg Phe Cys Arg Gly Lys Arg Trp 995 1000 1005 Ser Gly Ile Ala Arg Ala His Ala Phe Glu Glu Ala Thr Pro Glu 1010 1015 1020 Met Lys Leu Ser Ala Phe Leu Thr Ser Leu Pro Cys Asp Leu Gln 1025 1030 1035 Thr Ser Lys Met Tyr Lys Val Ala Asp Pro Tyr Phe Val Met Glu 1040 1045 1050 Met Leu His Glu Val Phe Lys Glu Ala Arg His Met Ala Thr Asn 1055 1060 1065 Ile Gln Asp Ala Ala Ala Phe Phe Lys Leu Ala Ser His Ser Val 1070 1075 1080 Ala Trp Met Leu Met Phe Gln Ala Ser Leu Gly Phe Arg Arg Ile 1085 1090 1095 Leu Met Pro Ala Asp Leu Ala Leu Leu Ile Phe Val Tyr Ile Pro 1100 1105 1110 Leu Met Gly Ser Cys Leu Leu Ser Asn Val Val Ala Glu Gly Thr 1115 1120 1125 Met Gln Gln Met Pro Ser Arg Cys Thr Lys Asp Asp Ala Lys Val 1130 1135 1140 Thr Ile Ala Ala Met Cys Lys Thr Tyr Pro Arg Leu Leu Leu Val 1145 1150 1155 Ala Thr Ser Leu Leu Val Phe Tyr Ser Phe Val Leu Gly Gln Ile 1160 1165 1170 Gln Ala Leu Leu Lys Ile Glu Leu Glu Arg Leu Tyr Asn Phe Thr 1175 1180 1185 Leu Asp Asp Thr Gln Cys Ser Arg Phe Trp Arg Val Ala Ser Tyr 1190 1195 1200 Ser Cys Leu Gln Glu His Glu Gln Ser Ile Ala Leu Leu Arg Thr 1205 1210 1215 Gln Val Gln Ser Val Ile Phe Arg Glu Asn Thr Ala Ala His Leu 1220 1225 1230 Ala Glu Gln Thr Ala Ser Phe Ala Met Ala Phe Leu Tyr Ser Val 1235 1240 1245 Ser Ser Ala Ser Trp Ile Val Arg Thr Gly Arg Ile Gly Ala Ile 1250 1255 1260 Ala Ser Glu Leu Leu His Ser Arg Trp Ile Ile Ser Ser Ala Ala 1265 1270 1275 Ile Leu Thr Ile Gln Gly Thr Ile Leu Val Ala Arg Ile Leu Ala 1280 1285 1290 Gln Pro Val Pro Leu Ala Ser Leu Asn Ala Ile Met Pro Trp Gly 1295 1300 1305 Leu Val Cys Gly Met Leu Leu Gly Leu Ser Leu Ala Ile Leu Ala 1310 1315 1320 Val Asp His Leu His Lys Phe Tyr Ala Ala Arg Gln His Glu Met 1325 1330 1335 Asp Gln Lys Asn Val Glu Ser Lys Val Thr Ser Asp Leu Asp Ile 1340 1345 1350 Met Asp Val Thr Cys Ile Cys Glu Pro Ile Leu Ser Pro Ser Thr 1355 1360 1365 Gln Lys Ile Ser Lys Arg Thr Ser Pro Pro Pro Ile Lys Gln Asn 1370 1375 1380 Val Arg Gly Ile Leu Gln Cys Lys Lys Arg Ser Tyr Thr Ser Lys 1385 1390 1395 Ser Asn Arg Arg Arg His Pro Ala Ile Phe Asn Pro Asp Thr Thr 1400 1405 1410 Ser Ala Lys Asp Met Gly Val Leu Arg Thr Arg Gln His Tyr Thr 1415 1420 1425 Ser Ile Leu Leu His Phe Leu Gln Arg Gly Ile Asn Gly Glu Gln 1430 1435 1440 Leu Gln Leu Val Ser Leu Asp Ile Asp Gln Glu Ser Phe Arg Leu 1445 1450 1455 Pro Leu Lys Lys His Ser Phe Gly Glu Glu Ala Ala Pro Ala Phe 1460 1465 1470 Leu Asp Val Tyr Val Glu Glu Asp Ile Gln Lys Ile Pro Val Met 1475 1480 1485 Phe Asn Leu Val Ile Glu Thr Lys Gly Asp Tyr Thr Tyr Arg Asn 1490 1495 1500 Tyr Phe Phe Lys Arg Asp Gly Asp Lys Phe Ile Asn Phe Asp Val 1505 1510 1515 Pro Lys Leu Ser Asp Tyr Tyr Asn Val Arg Thr Glu Gly Ile Ala 1520 1525 1530 Thr Tyr Tyr Leu Thr Tyr Lys Pro Ile Arg Val Pro Arg Glu Val 1535 1540 1545 Leu Lys Arg Leu Arg Arg Glu Phe Pro Asp Asn Asn Gln Leu Lys 1550 1555 1560 Val Ser Asn Asp Pro Glu Asp Gly Pro Arg Ser Asn Glu Ile Thr 1565 1570 1575 Leu Lys Leu Lys Leu Asn Ser Gly Ser Leu Val Ser Tyr Met Gly 1580 1585 1590 Thr Tyr Val Pro Lys Thr Ser Ser Arg Gly Cys Arg Ser Lys Ala 1595 1600 1605 Pro Ile Phe Asn Lys Phe Arg Tyr Lys Leu Thr Thr Asp Gly Gln 1610 1615 1620 Ala Ile Pro Val Asp Glu Val Glu Glu Glu Gly Glu Glu Glu Glu 1625 1630 1635 Glu Glu Asn Glu Asn Glu Lys Thr Glu Glu Thr Asp Asp Gln Asp 1640 1645 1650 Arg Lys Val Val Thr Lys Glu Asp Asp Glu Glu Glu Glu Asp Glu 1655 1660 1665 Glu Val Glu Glu Val Glu Glu Glu Leu Val Glu Ile Lys Asp Glu 1670 1675 1680 Glu Glu Asp Lys Cys Tyr Ile Glu Ala Trp Glu Lys His Ser Lys 1685 1690 1695 Asn Tyr Ser Lys Val Glu Val Ala Thr Ser Asn Lys Lys His Ile 1700 1705 1710 Ser Asp Thr Gly Ser Leu Lys Pro Ile Asp Glu Leu Ser Gly Leu 1715 1720 1725 Phe Asn Ala Leu Glu Arg Lys Ile Ala Thr Glu Thr Ala Leu Glu 1730 1735 1740 Ser Asp Thr Thr Tyr Thr Pro Lys Asp Asn Glu Arg Trp Ile Ile 1745 1750 1755 Asp Lys Cys Asn Ser Glu Glu Ser Ile Leu Asp Leu His Ile Lys 1760 1765 1770 Glu Asp Ile Leu Thr Phe Asp Val Pro Ile Thr Gln Leu Pro Ile 1775 1780 1785 Gln Glu Lys Glu Ile Val Asp Pro Cys Asn Ser Gln Arg Lys Ser 1790 1795 1800 Ala Phe Phe Asn Lys Ile Gly Ser Ala Gly Glu His Tyr Leu Arg 1805 1810 1815 Ala Phe Gly Ser Asn Ile Leu Ser Val Ile Asp Ile Met Lys Ser 1820 1825 1830 Asp Leu Asn Val Ser Ile Lys Lys Val Asn Ser Asp Glu Ile Asn 1835 1840 1845 Glu Asp Leu Pro Thr Lys Glu Lys Leu Leu Ala Met Glu Pro Ile 1850 1855 1860 Met Phe Asn Ser Met Asp Gly Glu Asp Asn Asn Asn Lys Asn Thr 1865 1870 1875 Asp Glu Glu Val Asn Gly Thr Lys Thr Leu Met His Ser Ile Asn 1880 1885 1890 Ser Gln Ser Ile Glu Arg Cys Glu Met Asn Ser Ala Tyr Asn Gln 1895 1900 1905 Gly Ser Phe Ile Ser Ile His Asp Gly Thr Ser Asp Ser Phe Met 1910 1915 1920 Asp Ser Asp Ser Phe Ser Ile Ser Gln Lys Ile Thr Gln Asp Glu 1925 1930 1935 Leu Leu Ser Lys His Asp Asp Lys Thr Leu Leu Asn Thr Asp Asn 1940 1945 1950 Ala Leu Asn Asp Asp Ser Gly Leu Lys Thr Thr Glu Ile Ser His 1955 1960 1965 Thr Val Asn Asp Thr Val Ile Pro Asn Leu Lys Leu Glu Lys Leu 1970 1975 1980 Leu Pro Gln Ser Lys Glu Gln Ser Ala Glu Ser Thr Ser Ser Gly 1985 1990 1995 Glu Val Gly Leu Ile Lys Lys Asn Lys Asp Val Gln Ser Thr Lys 2000 2005 2010 Gly Lys Val Gly Asp Leu Gly Asn Tyr Val Gln Ile Asn Asp Asp 2015 2020 2025 Lys Glu His Pro Arg Glu Ile Val Thr Val Glu Lys Phe Ala Asp 2030 2035 2040 Glu Thr Gly Ile Gly Thr Ser Thr Lys Lys Asn Glu Pro Ala Thr 2045 2050 2055 Thr Ser Pro Leu Asn Glu Phe Asp Lys Ile Pro Asn Asn Asp Ala 2060 2065 2070 Ala Val Asn Asp Ser Glu Lys Lys Thr Pro Ala Asp Glu Ser Arg 2075 2080 2085 Gly Asn Thr Asn Ala Lys Lys Thr Ser Asp Gly Asn Phe Lys Thr 2090 2095 2100 Ile Ser Ala Asn Leu Lys Pro Leu Lys Pro Phe Arg Pro Asp Ser 2105 2110 2115 Leu Val Thr Ala Met His Ile Ser Asn Asp Asn Lys Phe Leu Ala 2120 2125 2130 Thr Gly Asn Glu Asn Gly Glu Leu Tyr Val Trp Lys Phe Glu Ser 2135 2140 2145 Ala Lys Met Met Ser Ser Pro Glu Ile Ser Asp Asn Arg Ile Asn 2150 2155 2160 Ala Leu Pro Lys Met Leu Asn Trp Glu Met Leu Ser Ser Thr Pro 2165 2170 2175 Thr Ala Gly Val Gln Ala His Glu Phe Phe Ile Tyr Ser Ile His 2180 2185 2190 Ile Ser Lys Ile Gln Asn Arg Lys His Ser Gly Ser Val Leu Val 2195 2200 2205 Val Thr Ser Gly Gly Asn Asn Tyr Val Arg Ile Trp Ala Leu Thr 2210 2215 2220 Lys Ser Asp Lys Glu Asn Val Leu Ile Leu Lys Gly Asp Arg Gln 2225 2230 2235 Phe Asp Asp Asp Ile Leu Thr Ala Phe Gln Leu Pro Ile Ser Gln 2240 2245 2250 His Ile Ala Ile Cys Gly Ile Asp Gln Val Ile Glu Ile Trp Lys 2255 2260 2265 Phe Pro Pro Ile Thr Thr Ser Val Asn Asp Asn Pro Lys Asn Ile 2270 2275 2280 Ser Ser Trp Asn Lys Thr Lys Glu Arg Ile Asp Val Glu Leu Thr 2285 2290 2295 Ile Gln Ser Val Ser Tyr Ser Pro Ser Gly Met Tyr Ile Ala Ile 2300 2305 2310 Gly Ser Ile Asp Gly Leu Leu Ser Leu Tyr Ser Ala Glu Thr Met 2315 2320 2325 Lys Leu Ile Ser Met Ala Ile Cys Arg Asn Glu Lys Gly Trp Tyr 2330 2335 2340 Ser Asn Ser Ala Ser Ile Thr Gly Ile Val Trp Asn Thr Lys Glu 2345 2350 2355 Thr Leu Val Cys Ala Thr Thr Ala Asp Ser Arg Ile Arg Leu Phe 2360 2365 2370 Ser Thr Asn Ile Glu Asn Asp Asn Ala Leu Ile Tyr Ala Glu Lys 2375 2380 2385 Leu Lys Gly His Lys Tyr Cys Gly Glu Asn Val Ala Ala Arg Phe 2390 2395 2400 Thr Gly Leu Asn Asp Glu Tyr Val Ile Cys Ile Ser Lys Gly Gly 2405 2410 2415 Tyr Ile Val Ile Trp Lys His Ser Cys Thr Glu Glu Arg Ile Phe 2420 2425 2430 Tyr Asp Gly Asn Pro Ile Ile Lys Asn Thr Asn Tyr Cys Lys Phe 2435 2440 2445 Lys Ile Ile Pro Lys Pro Tyr Ile Gly Lys Leu Leu Gly Val Phe 2450 2455 2460 Asn Pro Gly Thr Trp Gly His Leu Trp Pro Thr Tyr Gln Glu Gln 2465 2470 2475 Ser Val Tyr Glu Pro Leu Asn Asp Lys Asn Ser Val Gly Cys Leu 2480 2485 2490 Asp Arg Phe Leu Thr Lys Asn Thr Pro Gly Val Lys Phe Ser Lys 2495 2500 2505 Ala Asn Pro Lys Asn Ala Ile Leu Leu Val Ala Ser Val Asp Gly 2510 2515 2520 Ser Gln Leu Leu Cys Thr Ile Ile Asp Ala Ser Leu Leu Val Phe 2525 2530 2535 Lys Lys Ser 2540 <210> 5 <211> 2541 <212> PRT <213> babesia duncani <400> 5 Met Ile Ser Ser Pro Pro Ser Gly Phe Ser Leu His Gly Glu Asp Ala 1 5 10 15 Lys Gly Thr Pro Arg Asp Val Glu Arg Gln Asp Ser Asp Arg Leu Asp 20 25 30 Pro Gly Asn Phe Pro Pro Asp Lys Tyr Trp Ser Pro Ser Ile Gly Leu 35 40 45 Ser Thr Ile Glu Ala Asn Arg Arg Val Val Trp Leu Leu Gln Glu Ala 50 55 60 Ile Ser Arg Tyr Lys Ile His Leu Gly Tyr Trp Asn Thr Thr Lys Ser 65 70 75 80 Cys Leu Thr Ile Asp Ile Leu Ile Gly Val Leu Val Leu Val Leu Phe 85 90 95 Ile Leu Gly Ala Glu Pro Asn Leu Gly Val Trp His Val Val Arg Pro 100 105 110 Val Leu Leu Leu Pro Trp Leu Val Leu Asn Cys Tyr Ser Lys Ile Thr 115 120 125 Val Met Arg Ile Lys Ser Ser Arg Ala Cys Glu Arg Val Arg Asp Val 130 135 140 Leu Glu Ser Phe Ser Arg Glu Leu Lys Thr Gly Gly His Thr Glu Val 145 150 155 160 Glu Gln Arg Arg Phe Ser Phe Asp Pro Pro Asn Ser Leu Leu Ile Pro 165 170 175 Val Tyr Arg Asp Arg Glu Trp Lys Arg Leu Pro Ala Asn Val Leu Leu 180 185 190 Ala Gly Asp Val Phe Lys Leu Gln Ile Gly Asp Tyr Phe Pro Cys Asn 195 200 205 Cys Arg Ile Ile Leu Ser Cys Asp Arg Glu Gly Lys Val Gln Leu Asp 210 215 220 Ala Asn Leu Phe Asn Ala Gly Ser Val Phe Lys Ser Ser His Leu Pro 225 230 235 240 Ser Ile Asn Thr Asn Asp Gly Gly Glu Trp Thr Asp Ala Ser Phe Val 245 250 255 Ala Val Thr Asp Ser Phe Val Gln Ser Leu Glu Thr Phe Leu Ser Ala 260 265 270 Asp Gln Gly Pro Gln Ser Arg Phe Met Phe Phe Asn Glu Arg Asp Trp 275 280 285 Glu Asn Cys Gln Lys Gly Pro Asn Thr Pro Pro Pro Thr Thr Cys Val 290 295 300 Trp Asn Phe Ser Asp Tyr Thr His Phe Ser Lys Tyr Gly Val Asp Trp 305 310 315 320 Ile Gln Leu Gly Ile Ala Phe Phe Ile Ser Ser Ile Val Thr Val Leu 325 330 335 Gln Ile Ile Trp Ser Gly Phe Gln Gly Trp Arg Arg His Val Asn Val 340 345 350 Phe Ala Thr Cys Ile Ile Cys Leu Cys His Pro Ala Phe Asp Pro Phe 355 360 365 Leu Asn Leu Ala Asp Ile Trp Gly Asn Val Lys Leu Gln Ser Leu Phe 370 375 380 Gln Trp His Asn Glu Lys Arg Phe Thr Val Asp Ile Leu Pro Gln Gln 385 390 395 400 Ser Ser Ser Ser Ser Ser Thr Phe Asp Ser Gly Ser Ser Glu Asp Ser 405 410 415 Val Asp Ser Glu Met Ala Ala Ser Arg Ile Pro Leu Leu His Gln Leu 420 425 430 Arg Glu Leu Asn Arg Val Phe Lys Arg Gly Leu Asp Ser Glu Gly Ser 435 440 445 Leu Leu Arg Thr Leu Cys Ser Val Thr Leu Leu Cys Phe Val Asp Asp 450 455 460 Met Gly Leu Leu Thr Glu Gly Cys Ala Thr Pro Gln Glu Leu Ala Val 465 470 475 480 Val Asp Pro Ser Gly Gly Ile Gly Thr Gln Arg Arg Gln Gln Lys Glu 485 490 495 Ser Thr Ala Met Phe Gln Ser Gly Asn Ile Asp Ala Ile Glu Thr Ile 500 505 510 Asn Ser Thr Ala Thr Ser His Lys Asp Ser Ile Gly Gln Thr Glu Gln 515 520 525 Ser Asp Lys Gly Thr Ile Lys Ala Gly Pro Arg Glu Gly Lys Gln Val 530 535 540 Val Arg Lys Asp Pro Gln Gly Gly Glu Arg Leu Val Ile Leu Asp Val 545 550 555 560 Phe Glu Asp Ser Ser Gln Tyr Tyr Lys Gln Tyr Val Lys Phe Asn Asn 565 570 575 Asp Ala Glu Arg Asn Cys Ile Pro Gln Val Leu Ser Leu Ser Phe Ala 580 585 590 Met Ser Ala Thr Gln Phe Pro Arg Val Gln Pro Ser Leu Leu Gln Leu 595 600 605 Lys Ala Ala Pro Asp Leu Ile His Thr Tyr Met Gly Met Leu Ala Asn 610 615 620 Gly Thr Leu His Asp Phe Thr His Cys Leu Cys Ala Phe Ala Gly Ser 625 630 635 640 Val Gly Leu Lys Arg Ser Tyr Ile Arg Arg Phe Arg Leu Leu Arg Phe 645 650 655 Ile Val Val Leu Asp Glu Thr Leu Gly Thr Asn Gly Lys Met Leu Ile 660 665 670 Tyr Phe Leu Arg Asp Pro Arg Lys Gln Ile Val Gln Met Leu Val Lys 675 680 685 Ala Lys Pro Glu Thr Val Phe Asp Arg Ser Ile Asn Tyr His Asp Arg 690 695 700 Ala Arg Gly Ala Ile Leu Pro Val Ser Arg Leu Thr Lys Arg Lys Leu 705 710 715 720 Arg Asp Leu Asn Met Gln Trp Val Ser Ser Gly Leu Thr Pro Phe Ala 725 730 735 Phe Ile Tyr Lys Pro Ile His Leu Asp Glu Phe Asn Leu Ile Met Ala 740 745 750 His Leu Pro Gly Val Ala Val Phe Lys Val Gly His Phe Leu Lys Leu 755 760 765 Asp Arg His Gln Ser Val Lys Tyr Gln Glu Ser Thr Thr Cys Gln Gln 770 775 780 Asp Pro Gln Ala Asp Tyr Phe Gly Glu Gly Gly Lys Ser Asp Ala Lys 785 790 795 800 Ala Arg Arg Trp Tyr Ala Arg Leu Thr Asp Tyr Asp Ala Ile Ser Met 805 810 815 Arg Tyr Gly Ser Met His Thr Asp Leu Arg Gln Arg Ile Leu Thr Asn 820 825 830 Ser Ile Gly Gly Leu Val Asn Ser Cys Leu Lys Asn Ser Ile Leu Leu 835 840 845 Gly Met Cys Ala Thr Lys Tyr Gln Tyr Pro Lys Glu Val Pro Ser Arg 850 855 860 Ile Gln Ser Phe His Glu Ala Gly Ile Arg Phe Val Tyr Phe Ser Lys 865 870 875 880 His Asp Glu Lys Gln Thr Arg Ile Val Gly Gly Leu Leu Gly Leu Glu 885 890 895 Thr Ser Trp Asn Ser Met Ile Ser Leu Val Lys Ser Gly Arg Tyr Ser 900 905 910 His Val Asn Gln Asp Gly Arg Val Val Leu Pro Ser Gly Ile Asp Asn 915 920 925 Ile Arg Arg His Ile Arg Asp Val Asp Asp Ile Pro Leu Gln Val Ser 930 935 940 Leu Phe Cys Asp Cys Thr His Thr Ser Thr Val Glu Met Met Arg Ile 945 950 955 960 Leu Arg Glu Asn Gly Glu Arg Ile Met Cys Val Gly Asn Gly Leu Arg 965 970 975 Pro Ser Asn Phe Phe Val Phe Cys Glu Ala His Ser Ser Val Ser Val 980 985 990 Ala Leu Gly Tyr His Pro Thr Cys Arg Phe Cys Arg Gly Lys Arg Trp 995 1000 1005 Ser Gly Ile Ala Arg Ala His Ala Phe Glu Glu Ala Thr Pro Glu 1010 1015 1020 Met Lys Leu Ser Ala Phe Leu Thr Ser Leu Pro Cys Asp Leu Gln 1025 1030 1035 Thr Ser Lys Met Tyr Lys Val Ala Asp Pro Tyr Phe Val Met Glu 1040 1045 1050 Met Leu His Glu Val Phe Lys Glu Ala Arg His Met Ala Thr Asn 1055 1060 1065 Ile Gln Asp Ala Ala Ala Phe Phe Lys Leu Ala Ser His Ser Val 1070 1075 1080 Ala Trp Met Leu Met Phe Gln Ala Ser Leu Gly Phe Arg Arg Ile 1085 1090 1095 Leu Met Pro Ala Asp Leu Ala Leu Leu Ile Phe Val Tyr Ile Pro 1100 1105 1110 Leu Met Gly Ser Cys Leu Leu Ser Asn Val Val Ala Glu Gly Thr 1115 1120 1125 Met Gln Gln Met Pro Ser Arg Cys Thr Lys Asp Asp Ala Lys Val 1130 1135 1140 Thr Ile Ala Ala Met Cys Lys Thr Tyr Pro Arg Leu Leu Leu Val 1145 1150 1155 Ala Thr Ser Leu Leu Val Phe Tyr Ser Phe Val Leu Gly Gln Ile 1160 1165 1170 Gln Ala Leu Leu Lys Ile Glu Leu Glu Arg Leu Tyr Asn Phe Thr 1175 1180 1185 Leu Asp Asp Thr Gln Cys Ser Arg Phe Trp Arg Val Ala Ser Tyr 1190 1195 1200 Ser Cys Leu Gln Glu His Glu Gln Ser Ile Ala Leu Leu Arg Thr 1205 1210 1215 Gln Val Gln Ser Val Ile Phe Arg Glu Asn Thr Ala Ala His Leu 1220 1225 1230 Ala Glu Gln Thr Ala Ser Phe Ala Met Ala Phe Leu Tyr Ser Val 1235 1240 1245 Ser Ser Ala Ser Trp Ile Val Arg Thr Gly Arg Ile Gly Ala Ile 1250 1255 1260 Ala Ser Glu Leu Leu His Ser Arg Trp Ile Ile Ser Ser Ala Ala 1265 1270 1275 Ile Leu Thr Ile Gln Gly Thr Ile Leu Val Ala Arg Ile Leu Ala 1280 1285 1290 Gln Pro Val Pro Leu Ala Ser Leu Asn Ala Ile Met Pro Trp Gly 1295 1300 1305 Leu Val Cys Gly Met Leu Leu Gly Leu Ser Leu Ala Ile Leu Ala 1310 1315 1320 Val Asp His Leu His Lys Phe Tyr Ala Ala Arg Gln His Glu Met 1325 1330 1335 Asp Gln Lys Asn Val Glu Ser Lys Val Thr Ser Asp Leu Asp Ile 1340 1345 1350 Met Asp Val Thr Cys Ile Cys Glu Pro Ile Leu Ser Pro Ser Thr 1355 1360 1365 Gln Lys Ile Ser Lys Arg Thr Ser Pro Pro Pro Ile Lys Gln Asn 1370 1375 1380 Val Arg Gly Ile Leu Gln Cys Lys Lys Arg Ser Tyr Thr Ser Lys 1385 1390 1395 Ser Asn Arg Arg Arg His Pro Ala Ile Phe Asn Pro Asp Thr Thr 1400 1405 1410 Ser Ala Lys Asp Met Gly Val Leu Arg Thr Arg Gln His Tyr Thr 1415 1420 1425 Ser Ile Leu Leu His Phe Leu Gln Arg Gly Ile Asn Gly Glu Gln 1430 1435 1440 Leu Gln Leu Val Ser Leu Asp Ile Asp Gln Glu Ser Phe Arg Leu 1445 1450 1455 Pro Leu Lys Lys His Ser Phe Gly Glu Glu Ala Ala Pro Ala Phe 1460 1465 1470 Leu Asp Val Tyr Val Glu Glu Asp Ile Gln Lys Ile Pro Val Met 1475 1480 1485 Phe Asn Leu Val Ile Glu Thr Lys Gly Asp Tyr Thr Tyr Arg Asn 1490 1495 1500 Tyr Phe Phe Lys Arg Asp Gly Asp Lys Phe Ile Asn Phe Asp Val 1505 1510 1515 Pro Lys Leu Ser Asp Tyr Tyr Asn Val Arg Thr Glu Gly Ile Ala 1520 1525 1530 Thr Tyr Tyr Leu Thr Tyr Lys Pro Ile Arg Val Pro Arg Glu Val 1535 1540 1545 Leu Lys Arg Leu Arg Arg Glu Phe Pro Asp Asn Asn Gln Leu Lys 1550 1555 1560 Val Ser Asn Asp Pro Glu Asp Gly Pro Arg Ser Asn Glu Ile Thr 1565 1570 1575 Leu Lys Leu Lys Leu Asn Ser Gly Ser Leu Val Ser Tyr Met Gly 1580 1585 1590 Thr Tyr Val Pro Lys Thr Ser Ser Arg Gly Cys Arg Ser Lys Ala 1595 1600 1605 Pro Ile Phe Asn Lys Phe Arg Tyr Lys Leu Thr Thr Asp Gly Gln 1610 1615 1620 Ala Ile Pro Val Asp Glu Val Glu Glu Glu Gly Glu Glu Glu Glu 1625 1630 1635 Glu Glu Asn Glu Asn Glu Lys Thr Glu Glu Thr Asp Asp Gln Asp 1640 1645 1650 Arg Lys Val Val Thr Lys Glu Asp Asp Glu Glu Glu Glu Asp Glu 1655 1660 1665 Glu Val Glu Glu Val Glu Glu Glu Leu Val Glu Ile Lys Asp Glu 1670 1675 1680 Glu Glu Asp Lys Cys Tyr Ile Glu Ala Trp Glu Lys His Ser Lys 1685 1690 1695 Asn Tyr Ser Lys Val Glu Val Ala Thr Ser Asn Lys Lys His Ile 1700 1705 1710 Ser Asp Thr Gly Ser Leu Lys Pro Ile Asp Glu Leu Ser Gly Leu 1715 1720 1725 Phe Asn Ala Leu Glu Arg Lys Ile Ala Thr Glu Thr Ala Leu Glu 1730 1735 1740 Ser Asp Thr Thr Tyr Thr Pro Lys Asp Asn Glu Arg Trp Ile Ile 1745 1750 1755 Asp Lys Cys Asn Ser Glu Glu Ser Ile Leu Asp Leu His Ile Lys 1760 1765 1770 Glu Asp Ile Leu Thr Phe Asp Val Pro Ile Thr Gln Leu Pro Ile 1775 1780 1785 Gln Glu Lys Glu Ile Val Asp Pro Cys Asn Ser Gln Arg Lys Ser 1790 1795 1800 Ala Phe Phe Asn Lys Ile Gly Ser Ala Gly Glu His Tyr Leu Arg 1805 1810 1815 Ala Phe Gly Ser Asn Ile Leu Ser Val Ile Asp Ile Met Lys Ser 1820 1825 1830 Asp Leu Asn Val Ser Ile Lys Lys Val Asn Ser Asp Glu Ile Asn 1835 1840 1845 Glu Asp Leu Pro Thr Lys Glu Lys Leu Leu Ala Met Glu Pro Ile 1850 1855 1860 Met Phe Asn Ser Met Asp Gly Glu Asp Asn Asn Asn Lys Asn Thr 1865 1870 1875 Asp Glu Glu Val Asn Gly Thr Lys Thr Leu Met His Ser Ile Asn 1880 1885 1890 Ser Gln Ser Ile Glu Arg Cys Glu Met Asn Ser Ala Tyr Asn Gln 1895 1900 1905 Gly Ser Phe Ile Ser Ile His Asp Gly Thr Ser Asp Ser Phe Met 1910 1915 1920 Asp Ser Asp Ser Phe Ser Ile Ser Gln Lys Ile Thr Gln Asp Glu 1925 1930 1935 Leu Leu Ser Lys His Asp Asp Lys Thr Leu Leu Asn Thr Asp Asn 1940 1945 1950 Ala Leu Asn Asp Asp Ser Gly Leu Lys Thr Thr Glu Ile Ser His 1955 1960 1965 Thr Val Asn Asp Thr Val Ile Pro Asn Leu Lys Leu Glu Lys Leu 1970 1975 1980 Leu Pro Gln Ser Lys Glu Gln Ser Ala Glu Ser Thr Ser Ser Gly 1985 1990 1995 Glu Val Gly Leu Ile Lys Lys Asn Lys Asp Val Gln Ser Thr Lys 2000 2005 2010 Gly Lys Val Gly Asp Leu Gly Asn Tyr Val Gln Ile Asn Asp Asp 2015 2020 2025 Lys Glu His Pro Arg Glu Ile Val Thr Val Glu Lys Phe Ala Asp 2030 2035 2040 Glu Thr Gly Ile Gly Thr Ser Thr Lys Lys Asn Glu Pro Ala Thr 2045 2050 2055 Thr Ser Pro Leu Asn Glu Phe Asp Lys Ile Pro Asn Asn Asp Ala 2060 2065 2070 Ala Val Asn Asp Ser Glu Lys Lys Thr Pro Ala Asp Glu Ser Arg 2075 2080 2085 Gly Asn Thr Asn Ala Lys Lys Thr Ser Asp Gly Asn Phe Lys Thr 2090 2095 2100 Ile Ser Ala Asn Leu Lys Pro Leu Lys Pro Phe Arg Pro Asp Ser 2105 2110 2115 Leu Val Thr Ala Met His Ile Ser Asn Asp Asn Lys Phe Leu Ala 2120 2125 2130 Thr Gly Asn Glu Asn Gly Glu Leu Tyr Val Trp Lys Phe Glu Ser 2135 2140 2145 Ala Lys Met Met Ser Ser Pro Glu Ile Ser Asp Asn Arg Ile Asn 2150 2155 2160 Ala Leu Pro Lys Met Leu Asn Trp Glu Met Leu Ser Ser Thr Pro 2165 2170 2175 Thr Ala Gly Val Gln Ala His Glu Phe Phe Ile Tyr Ser Ile His 2180 2185 2190 Ile Ser Lys Ile Gln Asn Arg Lys His Ser Gly Ser Val Leu Val 2195 2200 2205 Val Thr Ser Gly Gly Asn Asn Tyr Val Arg Ile Trp Ala Leu Thr 2210 2215 2220 Lys Ser Asp Lys Glu Asn Val Leu Ile Leu Lys Gly Asp Arg Gln 2225 2230 2235 Phe Asp Asp Asp Ile Leu Thr Ala Phe Gln Leu Pro Ile Ser Gln 2240 2245 2250 His Ile Ala Ile Cys Gly Ile Asp Gln Val Ile Glu Ile Trp Lys 2255 2260 2265 Phe Pro Pro Ile Thr Thr Ser Val Asn Asp Asn Pro Lys Asn Ile 2270 2275 2280 Ser Ser Trp Asn Lys Thr Lys Glu Arg Ile Asp Val Glu Leu Thr 2285 2290 2295 Ile Gln Ser Val Ser Tyr Ser Pro Ser Gly Met Tyr Ile Ala Ile 2300 2305 2310 Gly Ser Ile Asp Gly Leu Leu Ser Leu Tyr Ser Ala Glu Thr Met 2315 2320 2325 Lys Leu Ile Ser Met Ala Ile Cys Arg Asn Glu Lys Gly Trp Tyr 2330 2335 2340 Ser Asn Ser Ala Ser Ile Thr Gly Ile Val Trp Asn Thr Lys Glu 2345 2350 2355 Thr Leu Val Cys Ala Thr Thr Ala Asp Ser Arg Ile Arg Leu Phe 2360 2365 2370 Ser Thr Asn Ile Glu Asn Asp Asn Ala Leu Ile Tyr Ala Glu Lys 2375 2380 2385 Leu Lys Gly His Lys Tyr Cys Gly Glu Asn Val Ala Ala Arg Phe 2390 2395 2400 Thr Gly Leu Asn Asp Glu Tyr Val Ile Cys Ile Ser Lys Gly Gly 2405 2410 2415 Tyr Ile Val Ile Trp Lys His Ser Cys Thr Glu Glu Arg Ile Phe 2420 2425 2430 Tyr Asp Gly Asn Pro Ile Ile Lys Asn Thr Asn Tyr Cys Lys Phe 2435 2440 2445 Lys Ile Ile Pro Lys Pro Tyr Ile Gly Lys Leu Leu Gly Val Phe 2450 2455 2460 Asn Pro Gly Thr Trp Gly His Leu Trp Pro Thr Tyr Gln Glu Gln 2465 2470 2475 Ser Val Tyr Glu Pro Leu Asn Asp Lys Asn Ser Val Gly Cys Leu 2480 2485 2490 Asp Arg Phe Leu Thr Lys Asn Thr Pro Gly Val Lys Phe Ser Lys 2495 2500 2505 Ala Asn Pro Lys Asn Ala Ile Leu Leu Val Ala Ser Val Asp Gly 2510 2515 2520 Ser Gln Leu Leu Cys Thr Ile Ile Asp Ala Ser Leu Leu Val Phe 2525 2530 2535 Lys Lys Ser 2540 <210> 6 <211> 160 <212> PRT <213> babesia duncani <400> 6 Met Pro Ser Gln Gly Thr Val Lys Ala Gln Thr Gly Thr Thr Glu Val 1 5 10 15 Asp Asn Ala Asp Ser Ser Glu Glu Glu Ser Gln Lys Ser Gln Pro Glu 20 25 30 Ser Lys Ala Val Asn Gly Ile Ser Gly Thr Glu Ser Arg Asn Glu Asn 35 40 45 Ser Gln Ser Val Asp Thr Asn Ser Ser Gly Asp Thr Asn Pro Ser Gln 50 55 60 Ser Ala Gly Gly Ser Ala Pro Thr Thr Gly Asp Ser Lys Asn Gln Gln 65 70 75 80 Gly Lys Asn Val Asn Ala Glu Ser Ser Ser Asn Pro Asn Ser Glu Lys 85 90 95 Ser Val Ala Thr Gln Asp Ser Ser Thr Asp Gln Thr Gly Lys Thr Asp 100 105 110 Ser Ser Thr Thr His Thr Thr Thr Gly Asp Ser Val Glu Gln Lys Gly 115 120 125 Asp Asp Asn Thr Glu Thr Thr Asp Thr Ala Gln Asn Thr Ala Thr Glu 130 135 140 Glu Ala Thr Thr Gly Ser Gly Thr Glu Gly Ser Ala Asp Gln Thr Glu 145 150 155 160 <210> 7 <211> 132 <212> PRT <213> babesia duncani <400> 7 Met Ala Arg Phe Phe Ser Tyr Lys Lys Leu Ile Ala Phe Ala Ile Val 1 5 10 15 Ala Leu Ala Ser Leu Lys Glu Val Ser Phe Leu Gly Gly Cys Pro Tyr 20 25 30 Ala Leu Ala Val Ala Thr Thr Thr Thr Thr Gly Thr Asn Gly Ala Ala 35 40 45 Thr Gly Thr Asn Gly Ala Ala Thr Gly Thr Asn Gly Ala Gly Ala Asn 50 55 60 Asp Thr Ser Lys Asn Thr Ser Asp Pro Asn Thr Pro Ala Thr Pro Pro 65 70 75 80 Ser Ser Pro Glu Ser Asn Lys Asp Asn Ala Ala Gly Gly Ser Asp Gly 85 90 95 Gln Lys Pro Thr Gly Gln Asp Pro Gln Lys Pro Asn Ala Gly Asn Gly 100 105 110 Phe Ala Ala Thr Ser Val Ile Gly Ala Ala Thr Ile Gly Leu Leu Thr 115 120 125 Leu Ala Phe Asn 130 <210> 8 <211> 188 <212> PRT <213> babesia duncani <400> 8 Met Thr Lys Tyr Ser Gln Glu Pro Ser Asn Leu Ala Lys Ser Ala Lys 1 5 10 15 Ala Tyr Gly Ala His Leu Arg Val His Phe Lys Asn Thr Tyr Glu Thr 20 25 30 Gly Arg Ala Ile Gln Gly Lys Met Ile Leu Glu Ala Lys Arg Tyr Leu 35 40 45 Asn Asp Val Ile Glu His Lys Arg Cys Val Pro Phe Arg Lys Phe Asn 50 55 60 Gly Gly Val Gly Arg Cys Ala Gln Ala Lys Ala Phe Lys His Thr Gln 65 70 75 80 Gly Arg Trp Pro Glu Lys Ser Cys Arg Ile Leu Leu Asp Leu Leu Thr 85 90 95 Asn Leu Glu Ser Asn Ala Glu Ala Lys Gly Leu Asp Val Glu Asn Met 100 105 110 Val Ile Glu Asn Val Leu Val Asn Arg Ala Pro Leu Gly Arg Arg Arg 115 120 125 Ser Tyr Arg Ala His Gly Arg Ile Ile Pro Phe Leu Ser His Pro Cys 130 135 140 His Val Ala Leu Ile Ala Val Glu Lys Asp Glu Asn Val Pro Arg Phe 145 150 155 160 Thr Pro Glu Ala Ala Lys Thr Ile Lys Leu Asn Lys Arg Gln Ile Ala 165 170 175 Arg Met Arg Leu Cys Asn Gly Lys Gly Val Ala Lys 180 185 <210> 9 <211> 490 <212> PRT <213> babesia duncani <400> 9 Met Ile Ser His Tyr Cys Leu Leu Leu Leu Ala Ala Ala Thr Val Phe 1 5 10 15 Gly Gly Glu Ala Thr Val Thr Ile Glu Asp Ala Lys Ser Ala Thr Leu 20 25 30 Glu Ala Thr Thr Gly Val Pro Glu Val Ala Glu Gly Asp Val Ser Ile 35 40 45 Pro Arg Gly Val Val Thr Leu Thr Ala Asp Asp Leu His Lys Ser Ile 50 55 60 Glu Lys His Glu Ala Ile Met Ile Lys Phe Tyr Ala Thr Trp Cys Gly 65 70 75 80 His Cys Lys Ile Leu Ala Pro Glu Tyr Ile Lys Ala Ala Lys Ile Leu 85 90 95 Glu Glu Glu Asn Val Asn Val Val Leu Ala Glu Ile Asp Ala Val Ala 100 105 110 His Ser Asp Ala Val Ala Glu Phe Glu Ile Lys Gly Tyr Pro Thr Ile 115 120 125 Lys Phe Phe Lys Arg Gly Ile Pro Ile Asp Tyr Asn Ser Asp Arg Lys 130 135 140 Ala Glu Thr Ile Ala Ser Trp Cys Lys Glu Met Leu Asn Pro Ala Leu 145 150 155 160 Met Glu Thr Thr Asn Leu Glu Ala Glu Ile Ala Ser Arg Lys Ser Lys 165 170 175 Ile Ala Leu Val Ala His Gly Cys Asn Asp Lys Asp Glu Leu Cys Val 180 185 190 Leu Phe Glu Lys Leu Ala Glu Val His Arg Met Asp Ala His Phe Phe 195 200 205 Ser Val Ala Asp Ser Ser Ser Val Trp Phe Glu Val Arg His Val Gly 210 215 220 Asp Gly Thr Leu Lys Phe Asn Gly Leu Ser Pro Glu Glu Leu Ala Leu 225 230 235 240 Phe Val Lys Asp Glu Thr Leu Pro Leu Leu Asp Glu Ile Asn Pro Ala 245 250 255 Asn Tyr Ala Arg Tyr Thr Ser Ser Gly Lys Ser Ile Ser Trp Leu Cys 260 265 270 Ala Asn Thr Gln Asp Tyr Thr Lys Tyr Arg Ser Ser Ile Val Glu Val 275 280 285 Ala Lys Glu Met Arg Ser His Thr Val Phe Val Trp Leu Asp Thr Glu 290 295 300 Lys Phe Ser Ala Val Asn Glu Ala Phe Ala Ile Ser Lys Leu Pro Ala 305 310 315 320 Ile Ala His Gln Thr Met Lys Gly Arg Phe Ile Leu Ser Pro Asp Ala 325 330 335 Tyr Asp Phe Thr Ser Lys Ser Ala Met Leu Gln Phe Tyr Thr Asp Val 340 345 350 Glu Gln Gly Lys Ile Pro Leu Ser Phe Arg Ser Glu Ala Glu Pro Gln 355 360 365 Asp Ala Thr Glu Gly Pro Val Met Leu Val Val Gly Lys Thr Leu Gln 370 375 380 Gln Leu Phe Thr Gln Thr Asp Lys Ala Val Leu Leu Met Ile His Ala 385 390 395 400 Pro Tyr Cys Glu His Cys Arg Asn Phe Met Pro Val Phe Glu Asp Phe 405 410 415 Ala Lys Thr Ile Asp Ala Gln Ala Pro Leu Ile Val Ala Lys Leu Asp 420 425 430 Gly Asp Ala Asn Glu Ser Pro Leu Asp Tyr Val Ser Trp Glu Ala Phe 435 440 445 Pro Thr Val Leu Leu Phe Lys Ala Gly Asp Lys Gln Pro Ile Pro Phe 450 455 460 Lys Gly Thr Arg Thr Ile Glu Glu Leu Thr Ser Phe Val Gln Glu His 465 470 475 480 Val Thr Leu Ala Pro Val Lys Thr Glu Leu 485 490 <210> 10 <211> 350 <212> PRT <213> babesia duncani <400> 10 Met Val Glu Glu Leu Asp Gly Thr Lys Asn Glu Tyr Gly Phe Cys Lys 1 5 10 15 Ser Lys Leu Gly Ala Asn Ala Ile Leu Val Val Ser Met Ala Ala Ala 20 25 30 Arg Ala Ala Ala Ala His Leu Asn Ile Pro Leu Tyr Val His Leu Ala 35 40 45 Asn Leu Ala Gly Lys Pro Thr Asn Lys Phe Ile Leu Pro Val Pro Cys 50 55 60 Leu Asn Val Ile Asn Gly Gly Ser His Ala Gly Asn Met Leu Ala Met 65 70 75 80 Gln Glu Phe Met Ile Leu Pro Ile Gly Ala Gly Ser Phe Arg Glu Ala 85 90 95 Ile Gln Met Gly Ser Glu Val Tyr His Thr Leu Lys Lys Val Ile Ser 100 105 110 Ser Lys Tyr Gly Gln Asp Ala Thr Asn Ile Gly Asp Glu Gly Gly Phe 115 120 125 Ala Pro Asn Ile Lys Asn Ala Glu Glu Ala Leu Asp Leu Leu Leu Glu 130 135 140 Ala Phe Arg Ile Ala Gly Val Glu Gly Leu Phe Lys Ile Ala Met Asp 145 150 155 160 Val Ala Ala Ser Glu Phe Tyr Asp Lys Asn Thr Gly Met Tyr Asn Leu 165 170 175 Gly Phe Lys Gly Lys Glu Pro Gln Asn Lys Thr Gly Glu Glu Met Ile 180 185 190 Ser Tyr Tyr Lys Leu Leu Cys Ala Lys Tyr Pro Ile Cys Ser Ile Glu 195 200 205 Asp Pro Phe Asp Gln Asp Asp Phe Asp Ser Tyr Thr Lys Leu Thr Ala 210 215 220 Ala Ile Gly Glu Lys Val Gln Ile Val Gly Asp Asp Leu Leu Val Thr 225 230 235 240 Asn Pro Lys Arg Ile Glu Met Ala Leu Gly Lys Lys Ala Cys Asn Ala 245 250 255 Leu Leu Leu Lys Val Asn Gln Ile Gly Ser Val Thr Glu Ser Ile Asp 260 265 270 Ala Cys Lys Met Ala His Ala Asn Lys Trp Gly Val Met Val Ser His 275 280 285 Arg Ser Gly Glu Thr Glu Asp Thr Phe Ile Ala Asp Leu Val Val Ala 290 295 300 Leu Gly Thr Gly Gln Ile Lys Thr Gly Ala Pro Cys Arg Ser Glu Arg 305 310 315 320 Asn Ala Lys Tyr Asn Gln Leu Leu Arg Ile Glu Glu Glu Leu Gly Asn 325 330 335 Lys Cys Glu Tyr Ala Gly His Asn Phe Arg Thr Cys Gly Asn 340 345 350 <210> 11 <211> 126 <212> PRT <213> babesia duncani <400> 11 Met Glu Glu Trp Tyr Thr Tyr Ala Leu Arg His Val Asp Leu Asp Leu 1 5 10 15 Asp Asn Phe Phe Val Glu Phe Gly Glu Thr Ile Leu Glu Asp Tyr Thr 20 25 30 Arg Ile Tyr Pro Arg Ser Asn Val Phe Val Asp Asn Ile Arg Lys Gly 35 40 45 Ala Thr Leu Ile Thr Leu Ser Thr Glu His Lys Gly Leu Leu Phe Val 50 55 60 Glu Leu Arg Tyr Pro Arg Pro Gly Lys Asp Ser Val Met Asp Ile Ile 65 70 75 80 Tyr Lys Asn Trp Glu Asp Glu Glu Val Met Phe Ser Leu Val Trp Val 85 90 95 Phe Gly Asp Trp Val Pro Gln Asn Phe Leu Tyr Ser Gly Ile Leu Asp 100 105 110 Ser Gly Pro Glu Tyr Val Pro Val Arg Arg His Asp Ser Arg 115 120 125 <210> 12 <211> 131 <212> PRT <213> babesia duncani <400> 12 Met Gln Ile Phe Val Lys Thr Leu Thr Gly Lys Thr Ile Thr Leu Glu 1 5 10 15 Val Glu Pro Ser Asp Thr Ile Glu Asn Val Lys Ala Lys Ile Gln Asp 20 25 30 Lys Glu Gly Ile Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys 35 40 45 Gln Leu Glu Asp Gly Arg Thr Leu Ser Asp Tyr Asn Ile Gln Lys Glu 50 55 60 Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly Val Ile Glu Pro 65 70 75 80 Ser Leu Val Cys Gln Lys Tyr Asn Cys Glu Lys Met Val Cys 85 90 95 Arg Arg Cys Tyr Wing Arg Leu Pro Leu Arg Wing Thr Asn Cys Arg Lys 100 105 110 Lys Arg Cys Gly Arg Ser Gln Leu Arg Pro Lys Lys Ile Lys 115 120 125 Gly Gly Asn 130 <210> 13 <211> 218 <212> PRT <213> babesia dunkin <400> 13 Met Gly Asn Pro Gly Leu Ile Phe Ile Ala Leu Phe Lys Tyr Ser Phe 1 5 10 15 Asn Cys Tyr Tyr Thr Phe Leu Pro Phe Lys Phe Asp Asn Asn His Phe 20 25 30 Asp Val Pro Arg His Glu Asn Phe Leu Pro Arg Ala Thr Val Pro Arg 35 40 45 Phe Val Asp Ile Tyr Val Ser Ala Asp Asp Pro Arg Ile Pro Ile Leu 50 55 60 Val Asn Phe Val Thr Gly Gly Met Thr Thr Ser Gly Pro Asp Thr Arg 65 70 75 80 Pro Thr Asn Arg Asn Tyr Phe Phe Lys Arg Asp Gly Asn Lys Leu Val 85 90 95 Asn Tyr Lys Phe Thr Asn Lys Pro Asn Asp Thr Val Glu Asn Asn Asp 100 105 110 Ile Val Thr Arg Ile Ser Arg Glu Arg Val Thr Tyr Tyr Val Gly Thr 115 120 125 Ser Asn Pro Glu Asp Ile Ile Val Ala Thr Lys Asp Pro Gln Asn Asp 130 135 140 Leu Asn Gln Arg Glu Asn Ser Met Tyr Ala Ser Leu Ala Thr Leu Asp 145 150 155 160 Pro Lys Ala Thr Ile Pro Arg Ile Gly Leu Lys Thr Lys Ser Lys Tyr 165 170 175 Asn Lys Val Ala Leu Tyr Ser Asp Glu His Lys Glu Lys Ile Glu Ile 180 185 190 Ser Asn Ala Asp Ile Asp Gly Val Met His Glu Lys Leu Ile Leu Phe 195 200 205 Arg Tyr Arg Leu Val Lys Glu Tyr Arg Val 210 215 <210> 14 <211> 797 <212> PRT <213> babesia duncani <400> 14 Met Arg Asn Val Lys Lys Arg Thr Val Pro Phe Leu Trp Ile Ser Cys 1 5 10 15 Phe Val Leu Tyr Gly Ile Tyr Asn Val Glu Pro Ile Ala Leu Tyr Asn 20 25 30 Lys Asn Trp Val His Lys Arg Val Gly Phe Ile Ala Asn Leu Lys Gln 35 40 45 Pro Pro Cys Gly Ile Thr Phe Gln Gly Leu Thr His Glu Lys Ala Lys 50 55 60 Arg Gly Phe Lys Arg Tyr Ala Glu Gln Ser Ser Gln Val Lys Glu Ala 65 70 75 80 Ser Val Leu Phe Asp Thr Leu Ser Asn Thr Glu Val Leu Asp Glu Leu 85 90 95 Asp Ser Asn Asp Ala Ile Gln Asp Thr Pro Asp Pro Leu Glu Ser Glu 100 105 110 Thr Ile Ile Glu Val Glu Val Glu Asp Lys Gly Lys Lys Thr Phe Ser 115 120 125 Asp Ile His Asn Lys Leu Lys Gly Ser Ile Asn Lys Leu Pro Ser Thr 130 135 140 Phe Ala Val Met Lys Asp Leu Val Val Phe Ala Leu Asp Thr Met Glu Gln 145 150 155 160 Gln Gly Asn Glu Lys Ser Ile Lys Ser Ile Tyr Thr Ser Ser Ile Lys Lys 165 170 175 Lys Leu Ile Thr Glu Leu Asn Lys Asn Val Glu Glu Leu Lys Ser Asp 180 185 190 Leu Pro Lys Thr Lys Lys Arg Leu Tyr Ile Ser Phe Leu Lys Asn 195 200 205 Thr Val Asp Pro Phe Phe Glu Asp Gln Tyr Val Asn Pro Val Asp Phe 210 215 220 Lys Asn Tyr Phe Ser Leu Tyr Asp Asn Tyr Lys Gln Glu Tyr Arg Lys 225 230 235 240 Cys Met Lys Thr Tyr Arg and Gly 245 250 255 Leu Lys Arg Lys Leu Lys His Gly Ile Val Ser Thr Phe Leu Trp Pro 260 265 270 Phe Ala Lys Trp Ala Lys Asp Asn Asn Val Arg Tyr Lys Glu Pro Lys 275 280 285 Pro Ser Gln Leu Glu Asn Phe Glu Arg Leu Leu Lys Tyr Tyr Gly His 290,295,300 Glu Phe Glu Asn Val Tyr Phe Glu Gln Asn Ile Ala Met Val Arg Pro 305 310 315 320 Pro Gln Pro Lys Ala Arg Pro Pro Asn Lys Trp Ser Leu Ile Phe Leu 325 330 335 Gly Thr Gly Ser Arg Gln Pro Thr Asp Thr Arg Met Thr Ser Thr Met 340 345 350 Ala Phe Thr Glu His Asp Gly Gly Arg Ile Trp Leu Phe Asp Cys Gly 355 360 365 Glu Gly Thr Cys Ala Cys Met Gln Lys Leu Asn Leu Asn Pro Lys Ala 370 375 380 Val Asp Arg Ile Phe Ile Thr His Leu His Gly Asp His Cys Phe Gly 385 390 395 400 Leu Phe Ser Phe Ile Ser Asn Ser Ala Arg Ala Leu Pro Ile Thr Val 405 410 415 Tyr Gly Pro Ile Gly Ile Ser Lys Met Leu Ile Asp Ile Met Asn Phe 420 425 430 Thr Thr Thr Ser Val Leu Pro Lys Phe Val Val His Glu Leu Val Leu 435 440 445 His Pro Asp Asn Glu Lys His Lys Thr Gly Trp His Val Asn Tyr Pro 450 455 460 Ser Phe Gly Gly Tyr Ile Tyr Pro Gln Glu Ala Gly His Tyr Leu Val 465 470 475 480 Tyr Glu Asn Asp Thr Cys Lys Val Met Ala Ala Pro Leu Lys His Ile 485 490 495 Leu Pro Thr Val Gly Tyr Val Ile Lys Glu Lys Ser Lys Asn Glu Asn 500 505 510 Asp Ser Thr Lys Thr Gln Arg Lys Ile Val Ile Cys Gln Asp Ser Cys 515 520 525 Asp Ser Ser Lys Met Val Pro Ile Ser Met Asn Pro Asn Val Leu Ile 530 535 540 His Glu Ala Thr Thr Ser Thr Thr Ser Thr Ile Gly Ser Ser Leu Ile 545 550 555 560 Met Gln Leu Val Tyr Asn Phe Ser Lys Gly Lys Ile Asp Glu Ser Leu 565 570 575 Leu Ser Lys Ile Asn Asp Ile Ile Ser Gln Glu Glu Leu Arg Arg Ser 580 585 590 Cys Phe Ser Val Thr Phe Thr Thr Met Ala Met Lys Leu Arg Arg Lys 595 600 605 Cys Tyr Leu Ile Glu Arg Ser Tyr Ser Asn Leu Thr Lys Thr Leu Glu 610 615 620 Gln Asn Glu Leu Lys Ala Thr Glu Thr Glu Ser Asn Asn Ala Asp Met 625 630 635 640 Met Thr Asp Ile Tyr Asn Ile Val Gln Leu Val His Ala Ala Ser Lys 645 650 655 Ile Lys Ser Cys Ile Ala Glu Ala Lys Lys Ile Glu Ser Gln Leu Lys 660 665 670 Glu Leu Tyr Asp Ala Pro Lys His Leu Gly Pro Arg Ser Thr Trp Leu 675 680 685 Lys Ser Val Tyr Asn His Val Arg Asp Val Ile Glu Asn Asn Gly Asn 690 695 700 Thr Glu Thr Ser Ser Ser Pro Thr Ile Gln Ala Met Glu Ser Leu Lys 705 710 715 720 Asn Leu Leu Thr Lys Phe Trp Thr Thr Asn Lys Ser Met Gly Leu Leu 725 730 735 Phe Ser Leu Glu Ile Asn Leu Pro Glu Ala Ala Pro Lys Asp Trp Phe 740 745 750 Ser Leu Tyr Ser Lys Ser Val Arg Tyr Ser Gly His Ser Thr Pro Trp 755 760 765 Asp Allele Gly Lys Phe Allele Lys Allele Ile Asn Allele Ser Leu Tyr Leu 770,775,780 Thr His Leu Ser Ser Val Ser Leu His Val His Phe Tyr 785,790,795 <210> 15 <211> 380 <212> PRT <213> babesia dunkin <400> 15 Met Leu Leu Ser Cys Trp Phe Asn Leu Ile Ala Cys Phe Ile Cys Ile 1 5 10 15 How To Make Arg With Clean Thr And How To Make Arg 20 25 30 Leu Ile Asn Thr Asn Asn Served Asn Ile Lys Met Lys Ala Thr Gly Lys 35 40 45 Leu Ser Met His Phe Lys Asn Lys Gln Gly Leu Leu Ile Arg Thr 50 55 60 Tyr Ala Ala Glu Val Asp Lys Pro Lys Gly Ser Ala Ile Leu Val His 65 70 75 80 Gly Asn Lys Served His Phe Arg Ala Asp Phe Thr Asn Tyr Asn Val Asp 85 90 95 Phe Tyr Lys Asp Lys Tyr Gly Leu Glu Ser Val Asp Pro Asn Ile Val 100 105 110 Ile Arg Glu Met His Ala Ile Tyr Pro Asn Val Asp His Lys Ile Asp 115 120 125 Phe Asn Asn Asp Tyr Glu Phe His Tyr Ser Lys Leu Asp Gly Lys Asn 130 135 140 Ala Leu Asp Ile Thr Pro Arg Phe Thr Leu Asn Gly Ser Ile Val Glu 145 150 155 160 Tyr Leu Asn Gly Leu Gly Tyr Ser Ala Tyr Gly Leu Asp Leu Gln Ser 165 170 175 Gln Gly Met Ser Gln Gly His Asn Gly His Arg Asn Tyr Phe Lys Lys 180 185 190 Phe Asp Asp His Val Val Asp Val Ile Gln Phe Ile Asp Ile Ile Arg 195 200 205 Arg Asn Lys Phe His Asn Val Asn Glu Glu Trp Asp Pro Asn Val Leu 210 215 220 Gly Lys Asn Tyr Ser Leu Asn Lys Cys Phe Leu Met Gly Leu Ser Met 225 230 235 240 Gly Gly Asn Val Val Leu Arg Ala Ala Gln Ile Phe Lys Thr Leu Ser 245 250 255 Asp Phe Lys Ser Asn Ile Val Asp Gly Ile Val Cys Phe Ala Pro Met 260 265 270 Leu Asp Ile Asp Met His Phe Ser Gly Ala Phe Asn Gln Leu Ala Leu 275 280 285 Ala Ile Ala Lys Met Ile Val Thr Phe Cys His His Ser Thr Phe Met 290 295 300 Ile Asn Glu Lys Tyr Glu Ile Asp Thr Leu Asn Ser Phe Leu Arg Val 305 310 315 320 Asn Asp Pro Tyr Tyr Ile Thr Lys Thr Gln Thr His Lys Ala Ile Val 325 330 335 Ser Leu Leu Glu Ala Thr Arg Thr Leu Glu Lys Asn His Ser Lys Tyr 340 345 350 Pro Val Asp Met Pro Thr Leu Val Phe His Cys Lys Asp Asp Asn Val 355 360 365 Cys Asp Phe Lys Val Phe Thr Cys Asn Glu Met Ile 370 375 380 <210> 16 <211> 713 <212> PRT <213> babesia duncani <400> 16 Met Ala Asp Gly Met Asn Gln Glu Thr Tyr Ala Phe Asn Ala Asp Ile 1 5 10 15 Ser Gln Leu Leu Ser Leu Ile Ile Asn Ala Phe Tyr Ser Asn Lys Glu 20 25 30 Ile Phe Leu Arg Glu Leu Ile Ser Asn Ala Ser Asp Ala Leu Glu Lys 35 40 45 Ile Arg Tyr Glu Ala Ile Lys Asp Pro Ser Ile Thr Glu Asp Gln Pro 50 55 60 Glu Tyr Phe Ile Lys Leu Tyr Ala Asp Lys Asn Asn Asn Thr Leu Thr 65 70 75 80 Ile Glu Asp Ser Gly Ile Gly Met Thr Lys Ala Asp Leu Ile Asn Asn 85 90 95 Leu Gly Thr Ile Ala Lys Ser Gly Thr Lys Ala Phe Met Glu Ala Ile 100 105 110 Gln Ala Gly Thr Asp Met Ser Met Ile Gly Gln Phe Gly Val Gly Phe 115 120 125 Tyr Ser Ala Tyr Leu Val Ala Asp Lys Val Thr Val Val Ser Lys Asn 130 135 140 Asn Asn Asp Glu Gln Tyr Ile Trp Glu Ser Asn Ala Ser Gly His Phe 145 150 155 160 Thr Ile Thr Lys Asp Glu Ser Gly Glu Gln Leu Lys Arg Gly Thr Arg 165 170 175 Ile Ile Leu Ser Leu Lys Asp Asp Gln Thr Glu Tyr Leu Glu Glu Arg 180 185 190 Arg Leu Lys Glu Leu Val Lys Lys His Ser Glu Phe Ile Gly Phe Pro 195 200 205 Ile Gln Leu Ser Val Glu Lys Thr Thr Glu Thr Glu Val Thr Asp Asp 210 215 220 Glu Ala Glu Glu Ser Ala Asp Ala Glu Gly Glu Lys Asp Lys Ile Gln 225 230 235 240 Asp Val Thr Asp Lys Asp Glu Thr Glu Ala Lys Glu Gly Glu Glu Gly 245 250 255 Asp Lys Asp Lys Lys Lys Lys Lys Arg Lys Val Gln Asn Val Thr Arg 260 265 270 Glu Trp Glu Met Leu Asn Lys Gln Lys Pro Ile Trp Met Arg Ser Pro 275 280 285 Asn Glu Val Thr Asn Glu Glu Tyr Ala Ser Phe Tyr Lys Asn Leu Ser 290 295 300 Asn Asp Trp Glu Asp His Leu Ala Val Lys His Phe Ser Val Glu Gly 305 310 315 320 Gln Leu Glu Phe Arg Ala Leu Leu Phe Val Pro Lys Arg Ala Pro Phe 325 330 335 Asp Met Phe Glu Ser Arg Lys Lys Lys Asn Asn Ile Lys Leu Tyr Val 340 345 350 Arg Arg Val Phe Ile Met Asp Asp Cys Glu Glu Leu Ile Pro Glu Trp 355 360 365 Leu Gly Phe Ile Lys Gly Val Val Asp Ser Glu Asp Leu Pro Leu Asn 370 375 380 Ile Ser Arg Glu Val Leu Gln Gln Asn Lys Ile Leu Lys Val Ile Arg 385 390 395 400 Lys Asn Leu Val Lys Lys Cys Leu Glu Leu Phe Asn Glu Leu Thr Glu 405 410 415 Light Light Asp Asp Phe Light Light Phe Tyr Glu Gln Phe Ser Light Asn Leu 420 425 430 Lys Leu Gly Ile His Glu Asp Asn Ala Asn Arg Thr Lys Ile Ser Glu 435 440 445 Leu Leu Arg Phe Glu Thr Thr Lys Ser Gly Asp Glu Ala Ile Ser Leu 450 455 460 Arg Asp Tyr Val Asp Arg Met Lys Pro Glu Gln Lys Tyr Ile Tyr Tyr 465 470 475 480 Ile Thr Gly Glu Ser Lys Gln Ser Val Ala Asn Ser Pro Phe Leu Glu 485 490 495 Thr Leu Arg Gln Arg Gly Met Glu Val Ile Tyr Met Thr Asp Pro Ile 500 505 510 Asp Glu Tyr Ala Val Gln Gln Ile Lys Glu Phe Glu Gly Lys Lys Leu 515 520 525 Lys Cys Cys Thr Lys Glu Asn Leu Glu Leu Asp Asp Asp Glu Glu Ala 530 535 540 Asn Lys Asn Phe Glu Lys Leu Lys Glu Glu Met Glu Pro Leu Cys Lys 545 550 555 560 Leu Ile Lys Glu Ile Leu His Asp Lys Val Glu Lys Val Thr Cys Gly 565 570 575 Arg Arg Phe Thr Glu Ser Pro Cys Ala Leu Val Thr Ser Glu Phe Gly 580 585 590 Trp Ser Ala Asn Met Glu Arg Ile Met Lys Ala Gln Ala Leu Arg Asp 595 600 605 Pro Ser Ile Thr Ser Tyr Met Val Ser Lys Lys Thr Met Glu Leu Asn 610 615 620 Pro Arg His Ala Ile Val Arg Glu Leu Arg Gln Arg Ala Glu Ser Asp 625 630 635 640 Lys Thr Asp Lys Thr Leu Lys Asp Leu Val Trp Leu Leu Tyr Asp Thr 645 650 655 Ala Leu Leu Thr Ser Gly Phe Asn Leu Asp Ala Pro Ala Glu Phe Gly 660 665 670 Asn Arg Ile Tyr Lys Met Ile Lys Leu Gly Leu Ser Leu Asp Asp Asp 675 680 685 Val Ala Glu Ala Ser Leu Asp Glu Val Pro Ala Leu Asp Glu Val Pro 690 695 700 Val Asp Ser Arg Met Glu Glu Val Asp 705 710 <210> 17 <211> 193 <212> PRT <213> Babesia duncani <400> 17 Met Arg Thr Leu Ser Arg Leu Pro Pro Pro Gly Asp Pro Gly His Val 1 5 10 15 Ala Ser Phe Gln Glu Ile Ala Thr Phe Asn Ile Asp Glu Phe Leu Ala 20 25 30 Asn Ile Asp Lys Thr His Asp Gly Val Ser Gln Leu Gln Leu Pro Pro 35 40 45 Asn Leu Leu Glu Asn Leu Lys Gln Gly Ala Gly Ser Leu Leu Gln His 50 55 60 Leu Ala Glu Gln Ser Thr Gly Pro Phe Ala Thr His Asn Gln Pro Ser 65 70 75 80 Leu Ile Gly Ala Ser Gly Met Ala Val Ala Ala Pro Gln Met Gln Leu 85 90 95 Pro Gln Val Ala Met Ala Pro Gln Val Met Ala Ala Pro Gln Pro Gly 100 105 110 Met Pro Pro Ala Val Ala Met Pro Gln Met Thr Ser Gln Phe Ala Gly 115 120 125 Ala Pro Gly Gln Ala Leu Pro Val Ala Ala Gln Ala Val Pro Asn Met 130 135 140 Gln Ala Pro Ala Gly Pro Gln Leu Ala Ser Val Pro Ile Ser Asn Val 145 150 155 160 Ile Arg Gly Asn Asn Ile Ala Phe Pro Gly Ala Val Pro Asn Glu Glu 165 170 175 Leu Ala Met Glu Leu Val Met Lys Ile Thr Trp Ala Leu Leu Met His 180 185 190 Cys <210> 18 <211> 255 <212> PRT <213> babesia duncani <400> 18 Met Ser Glu Glu Asn Ser Gln Arg Ala Gln Leu Thr Tyr Ser Ala Lys 1 5 10 15 Leu Ala Glu Gln Ala Glu Arg Tyr Asp Glu Met Ala Asp Ala Met Lys 20 25 30 Leu Leu Val Glu Thr Cys Ile Thr Asp Lys Asp Glu Leu Thr Val Glu 35 40 45 Glu Arg Asn Leu Leu Ser Val Ala Tyr Lys Asn Ala Val Gly Ser Arg 50 55 60 Arg Ala Ser Trp Arg Ile Val Ser Ser Val Glu Gln Lys Glu Ala Ser 65 70 75 80 Lys Ser Asn Ser Val His Lys Thr Leu Ala Gly Glu Tyr Arg Ala Lys 85 90 95 Ile Glu Lys Glu Leu Asn Lys Ile Cys Leu Cys Ile Ile Gly Leu Leu 100 105 110 Asp Glu Lys Leu Ile Pro Ala Thr Val Asp Ser Glu Ser His Val Phe 115 120 125 Tyr Tyr Lys Met Lys Gly Asp Tyr Tyr Arg Tyr Ile Ser Glu Phe Ser 130 135 140 Cys Asp Glu Ser Lys Ala Asn Ala Ser Ala Ser Ala Arg Asp Ser Tyr 145 150 155 160 Gln Lys Ala Thr Glu Ile Ala Glu Ser Glu Leu Lys Ser Thr His Pro 165 170 175 Ile Arg Leu Gly Leu Ala Leu Asn Tyr Ser Val Phe Phe Tyr Glu Ile 180 185 190 Leu Asn Arg Pro Gln Gln Ala Cys Glu Met Ala Lys Arg Ala Phe Asp 195 200 205 Asp Ala Ile Thr Glu Phe Asp Ser Val Ser Glu Asp Ser Tyr Lys Asp 210 215 220 Ser Thr Leu Ile Met Gln Leu Leu Arg Asp Asn Leu Thr Leu Trp Cys 225 230 235 240 Ser Asp Val Thr Ser Asp Ala Pro Asp Lys Gln Lys Gln Glu Asp 245 250 255 <210> 19 <211> 742 <212> PRT <213> babesia duncani <400> 19 Met Phe Gly Leu Leu Arg Pro Cys Leu Ile Arg Leu Ser Gly Ala Val 1 5 10 15 Ala Thr Arg Gln Thr Phe Gly Asn Leu Ala Asp Cys Leu Lys Ile Ala 20 25 30 Glu Ser Ser Gln Ser Ile Ala Thr Thr Asp Leu Tyr Glu Ala Phe Lys 35 40 45 Phe Ile Ser Ser Ser Gly Gln Ile Arg Arg Gln Ala Ile His Asp Asp 50 55 60 Arg Phe Val Thr Leu Leu Asp Gln Leu Asp Ala Arg Ile Ser Thr Leu 65 70 75 80 Asn Cys Ser Tyr Met Gly Asn Phe Gly Ile Arg Leu Gly Leu Ile Ile 85 90 95 Gln Ser Leu Gly Asn Leu Asp Arg Glu Asp Pro Ile Val Glu Lys Ser 100 105 110 Val Lys Val Ile Glu Arg Leu Cys Thr Glu Met Met Glu Lys Ser Gly 115 120 125 Asn Ile Lys Glu Ile Ser Gln Leu Ala Phe Ala Ala Ala Ser Ala Gly 130 135 140 Leu Gln His Lys Phe Leu Asp Tyr Ala Lys Gln Asn Leu Thr Leu Asn 145 150 155 160 Ile Glu Asn Ala Asp Pro Asp Val Leu Asn Leu Ala Leu Leu Ala Ser 165 170 175 Tyr Lys Thr Lys Val His Asp Lys Val Phe Leu Ala Leu Ile Cys Glu 180 185 190 Lys Leu Ser Glu Leu Thr Asp Arg Phe Thr Ala Asn Asp Val Val Ser 195 200 205 Thr Leu Arg Ser Leu Glu Lys Thr Ser Leu Met Lys Gly Phe Leu Leu 210 215 220 Arg Arg Leu Ser Met Leu Ile His Asp Asn Leu Glu Gln Phe Thr Asn 225 230 235 240 Glu Gln Leu Ala Gln Cys Cys Tyr Arg Leu Ser Ile Leu Lys Phe Gln 245 250 255 Thr Pro Val Gln Tyr Ser Thr Ile Leu Ser Leu Leu Glu Pro Lys Phe 260 265 270 Gln Gln Leu Ser Ile His Leu Gln Ile Glu Val Leu Ala Ser Gly Cys 275 280 285 Met Cys Gln Cys Thr Asp Ala Asn Glu Arg Leu Val Lys Leu Ala Lys 290 295 300 Ser Ile Thr Leu Thr Asp Lys Val Asp Leu Ala Gly Leu Val Asn Tyr 305 310 315 320 Ile Tyr Ser Cys Val Tyr Leu Lys Leu Tyr Lys Gly Asp His Leu Thr 325 330 335 Gly Ala Leu Glu Glu Ala Leu Ala Arg Ser Pro Phe Leu Ile Arg Lys 340 345 350 Tyr Ala Leu Leu Phe Lys Glu Ala Tyr Asp Thr Leu Ser Leu Glu Cys 355 360 365 Pro Asn Leu Thr Leu Glu Leu Pro Glu Ala Trp Lys Met Ala Leu Glu 370 375 380 Asn Tyr Glu Ser Ala Glu His Asp Arg Cys Ile Gln Thr Ser Ile Ile 385 390 395 400 Ala Glu Thr Gly Asn Ile Leu Lys Thr Ser Ala Gly Asp Phe Glu Thr 405 410 415 Phe Ser Lys Val Gly Pro Phe Thr Val Ala Phe Ala Asp Val Ala Arg 420 425 430 Lys Leu Val Ile Leu Ala Glu Thr Pro Asn Thr Leu Gly Gly Leu Ala 435 440 445 Leu Ala Gln Arg Ser Ile Lys Ala Met Asp Tyr Lys Val Ala Ile Ile 450 455 460 Lys Tyr Trp Glu Trp Arg Arg Leu Lys Thr Glu Lys Ser Glu Leu Ser 465 470 475 480 Tyr Ala Phe Lys Arg Phe Asp Lys Ser Arg Leu Gly Val Leu Ser His 485 490 495 Val Gln Phe Val Arg Leu Leu Gly Ala Ile Gly Ile His Leu Thr Arg 500 505 510 Gln Glu Leu Lys Phe Leu Gln Phe Glu Glu Asp Ile Arg Gly Gly Phe 515 520 525 Thr Leu Glu Asp Leu Glu Ala Leu Gly Arg Asp Phe Tyr Asn Asp Glu 530 535 540 Val Ile Ala Thr Lys Val Leu Glu Ser Leu Gln Glu His Phe Gly Pro 545 550 555 560 Cys Asn Thr Leu Asp Lys Gln Glu Leu Ala Ser Val Leu Met Lys Leu 565 570 575 Gly Ala Ser Leu Gly Val Ala Arg Glu Glu Leu Asp Thr Phe Leu Asn 580 585 590 Phe Tyr Ser Ala His Ser Asn Ser Ile Ser Val Glu Ala Phe Ile Arg 595 600 605 Gly Ala Ala Leu Gly Val Leu Glu Leu Cys Ala Asp His Thr Val Thr 610 615 620 Ile Leu Gln Trp Glu Thr Ser Arg Leu Gln Thr Lys Thr Ser Lys Met 625 630 635 640 Ser Gly Arg Gly Lys Gly Gly Lys Gly Leu Gly Lys Gly Gly Ala Lys 645 650 655 Arg His Arg Lys Val Leu Arg Asp Asn Ile Gln Gly Ile Thr Lys Pro 660 665 670 Ala Ile Arg Arg Leu Ala Arg Arg Gly Gly Val Lys Arg Ile Ser Gly 675 680 685 Leu Ile Tyr Glu Glu Val Arg Gly Val Leu Lys Val Phe Leu Glu Asn 690 695 700 Val Ile Arg Asp Ala Val Thr Tyr Thr Glu His Ala Arg Arg Lys Thr 705 710 715 720 Val Thr Ala Met Asp Ile Val Tyr Ser Leu Lys Arg Gln Gly Arg Thr 725 730 735 Leu Tyr Gly Phe Gly Gly 740 <210> 20 <211> 400 <212> PRT <213> Babesia duncani <400> 20 Met Val Leu Ser Pro Ile Leu Gln Phe Ser Phe Leu Ala Leu Pro Ser 1 5 10 15 Met Leu Leu Asn Asn Val Phe Ala Leu Arg Met Ser Ala Pro Thr Pro 20 25 30 Ile Glu Ser Pro Val Thr Lys Tyr Gly Asp Ser Leu Asn Met Leu Phe 35 40 45 Leu Asp Leu Gly Asn Ala Phe His Glu Asn Phe Ser Met Phe Gln Val 50 55 60 Ala Thr Ser Met Ser Asn Tyr Ala Glu Thr Asn Asn Asp Ile Val Ser 65 70 75 80 Arg Ile Cys Glu Arg Phe Glu Ser Gln Lys Ala Cys Phe Val Leu Ala 85 90 95 Ser Lys Tyr Ile Asn Asn Cys Ala Lys Ala Lys Cys Met Gln Ile 100 105 110 Glu Lys Phe His Leu Phe Gln Ser Pro Asp Met Ser Ile Lys Leu Met 115 120 125 Asn Arg Ala Gln Leu Ala Ala Ala Ile His Val Phe Arg Asn Ser Gly 130 135 140 Val Tyr Glu Lys Asn Tyr Leu Lys Arg Arg Phe Asn Lys Ile Phe Lys 145 150 155 160 Arg Gln Pro Phe Gly Tyr Ser Ser Tyr Arg Thr Leu Leu Ile Pro Leu 165 170 175 Leu Tyr Ser Asn Ala Serves Phe Asn Glu Tyr Thr Thr Phe Ser Glu Ile 180 185 190 Phe Ile Thr Tyr Tyr Leu Asn Val Ala Thr Phe Met Tyr Ala Thr Leu 195 200 205 Ile Tyr Arg Asp Thr Arg Leu Ala Arg Phe Val Asn Ala Phe Asp Lys 210 215 220 Leo Asn Val Leo Leo Ile Pro Leo Lys Lys His Leo Arg Asn Met Val 225 230 235 240 Thr Gly Ile Ala Asn Ala Ser Pro Val Ala Phe Cys Glu Glu Asp Phe 245 250 255 Glu Pro Ile Leu Arg Ile Phe Gly His Tyr Leu Ser Gly Phe Asp Lys 260 265 270 Ser Leu Thr Pro Leu Ala Asn Arg Phe Ala Lys Leu Ile Arg Asp Val 275 280 285 Leu Lys Asn Glu Leu His Lys Ser Glu Ser Cys Ile Leu Asn Arg Ala 290 295 300 Gly Asp Phe Leu Lys Asn Ala Gly Arg Arg Ala Gly Lys Ala Val Arg 305 310 315 320 Asp Ala Gly Ala Thr Ile Lys Glu Arg Gly Met Ala Thr Tyr Lys Gly 325 330 335 Val Lys Gly Gly Leu Ala Gly Ala Ser Asp Lys Ile Arg Asn Arg Phe 340 345 350 Arg Ser Arg Asn Gly Asn Gly Asp Asp Ala Ser Ser Tyr Gly Leu Leu 355 360 365 Asp Glu Asp Ala Thr Gly Glu Ala Thr Asp Asp Val Lys Pro Glu Asp 370 375 380 Asp Ser Thr Gly Asp Asn Glu Pro Lys Glu Asp Glu Ile Thr Arg Leu 385 390 395 400 <210> 21 <211> 242 <212> PRT <213> babesia duncani <400> 21 Met Asn Leu Lys Trp Leu Leu Gly Leu Ala Leu Ile Gly Ser Lys Tyr 1 5 10 15 Ala Leu Gly Gly Asp Pro Asn Asp Ser Glu Val Asp Ser Gly Lys Glu 20 25 30 Arg Gly Pro Gly Lys Arg Met Thr Phe Asp Glu Leu Leu Asp Glu Leu 35 40 45 Lys Thr Ala Glu Ala Ser Val Leu Gly Ile Lys Ala Glu Ile Asn Gly 50 55 60 Gly Leu Asn Arg Leu Arg Tyr Arg Ile Gly Asn Leu Asp Ala Ile Thr 65 70 75 80 Lys Ser Asp Tyr Asp Glu Ile Ser Asp Ala Ile Arg Asp Ile Ile Thr 85 90 95 Lys Arg Thr Glu Phe Ala Lys Ala Val Asn Lys Arg Val Gln Leu Glu 100 105 110 Ala Ile Ala Asn Lys Phe Ser Glu Arg Thr Ser Met Gly Asn Leu Glu 115 120 125 Asp Ile Gln Phe Ser Thr Phe Trp Val Lys Leu Glu Ala Ile Thr Arg 130 135 140 Val Pro Asp Phe Gln Leu Lys Glu Asp Phe Val Lys Met Lys Asp Glu 145 150 155 160 Ile Ile Asp Val Lys Glu Lys Phe Ile Glu Lys Leu Lys Lys Ala Arg 165 170 175 Glu Ala Thr Ala Glu Val Ile Pro Glu Thr Ile Val Glu Asp Gln Glu 180 185 190 Met Lys Ser Asp Leu His Glu Glu Ile Lys Ser His Gly Asp Asp Asp 195 200 205 Ile Phe Asn Asp Lys Ser Asp Lys Lys Gln Asn Ser Gly Phe Ala Ala 210 215 220 Thr Ser Ser Ser Leu Ile Leu Leu Ala Met Ala Thr Ile Gly Tyr Ser 225 230 235 240 Leu Phe <210> 22 <211> 917 <212> PRT <213> babesia duncani <400> 22 Met Ala Lys Ser Ala Leu Tyr Ile Leu Asp Ser Asn Val Lys Ser Lys 1 5 10 15 Lys Val Asp Lys Glu Ser Leu Lys Leu Ile Lys Lys Gln Ser Gly Lys 20 25 30 Pro Lys Lys Ile Leu Arg Pro Val Glu His Lys Ala His Asn Pro Ser 35 40 45 Cys Leu Glu Asn Ala Lys Val Glu Leu Asp Leu Asp Leu Leu Lys Lys 50 55 60 Val Ile Glu Thr Leu Lys Lys Arg Ala Glu Val Val Arg Glu Ser Asn 65 70 75 80 Thr Arg Asp Leu Leu Glu Asp Pro Ser Arg Asn Tyr Val Phe Ile Gln 85 90 95 Ile Ala Leu Thr Lys Val Val Thr Glu Val His Val Lys Pro Leu Gln 100 105 110 Ile Lys Leu Lys His Pro Ile Tyr Thr Asp Lys Glu Val Cys Ile Phe 115 120 125 Val Lys Asp Pro Gln Lys His Trp Lys Glu Ile Ile Lys Arg Glu Asn 130 135 140 Val Pro Gln Ile Lys Lys Val Ile Gly Val Thr Lys Leu Lys Lys 145 150 155 160 Tyr Lys Gln Phe Glu Asp Arg Arg Lys Leu Cys Arg Ser Phe Asp Leu 165 170 175 Phe Leu Cys Asp Lys Ala Val Cys Cys Ser Leu Pro Ser Leu Leu Gly 180 185 190 Lys Val Phe Ile Gln Arg Lys Lys Met Pro Val Pro Ile Ser Met Ser 195 200 205 Lys Gly Gly Leu Gly Asn Ser Met Arg Glu Ala Ile Gln Ser Thr Tyr 210 215 220 Tyr Lys Leu Ser Thr Gly Asn Thr Cys Ser Val Lys Val Gly Ile Cys 225 230 235 240 Ser Met Asn Thr Glu Gln Leu Ile Asp Asn Ile Lys Gln Val Phe Gln 245 250 255 Thr Ile Lys Lys Phe His Thr Glu Asp Pro Ile Phe Arg Asn Val Ile 260 265 270 Ser Ser Ile Phe Leu Asn Trp Glu Gly Thr Glu Ser Leu Met Leu Tyr 275 280 285 Ser Arg Ala Leu Ala Asp Asp Asp Ile Gln Ile Pro Gln Ser His Val 290 295 300 Thr Ser Pro Ser Lys Pro Thr Ala Ala Lys Pro Thr Cys Lys Trp Phe 305 310 315 320 Gly Thr Ser Gln Ser Asp Leu Val Ala Arg Ile Val Ala Thr Ala Lys 325 330 335 Gly Gly Thr Thr Ser Leu Ser Val Trp Arg Gln Phe Ser Lys Asp Val 340 345 350 Ile Glu Thr Ile Asp Thr Leu Asn Ile Pro Asp Val Tyr Arg Ile Leu 355 360 365 Lys Cys Phe Ser Ile Leu Arg Tyr Arg His Asp Pro Leu Leu Asn Val 370 375 380 Ile Ser Tyr Arg Ile Val Glu Ser Leu Asp Lys Ile Ala Cys Lys Asn 385 390 395 400 Leu Ala Glu Ile Leu Lys Ala Tyr Ser Lys Leu Glu Cys Arg Asn Asp 405 410 415 Phe Leu Leu Lys Thr Ala Leu Pro Thr Val Ala Arg His Leu Glu Phe 420 425 430 Phe Thr Pro Ser Asp Leu Ser Ser Val Phe Tyr Ser Tyr Cys Asn Leu 435 440 445 Gly Phe His Asp Leu Asn Phe Ile Arg Gln Val Glu Trp Arg Ile Phe 450 455 460 Asn Thr Leu Gly Lys Leu Gln Ser Cys Asp Phe Ala Leu Leu Phe Cys 465 470 475 480 Gly Leu Thr Arg Leu Glu Arg Ile Asn Thr Arg Phe Val Ile Ser Leu 485,490,495 Ala Cys Gln Phe Cys Lys Ser Leu Asp Ala Ile Asp Glu Lys His Phe 500 505 510 Ser Leu Cys Val Asn Ala Leu Gly Arg Leu Glu Phe Ala Glu His Pro 515,520,525 His Tyr Gly Ile Leu Val Gln His Tyr Asn Glu Ile Lys Lys 530 535 540 His His Leu Thr Ser Val Ser Leu Ala Leu Leu Val Asn Gly Phe Ser 545 550 555 560 Arg Ala Lys Pro Lys Asp Leu Lys Val Phe Gln Met Leu Ser Lys Gln 565,570,575 Glu Ser Arg Ser Glu Phe Asp and His Ser Cys Leu 580,585,590 Thr Only Gly Tyr Ser Arg With Asn Only Met Gln Val Tyr Leu 595,600,605 Phe Glu Lys Ile Ala Glu Ser Val Gly Arg Lys Ser Leu Gln Leu Tyr 610 615 620 Pro Met Ala Ile Thr Ser Leu Met Tyr Ser Phe Ser Arg Ala Gly His 625 630 635 640 Val His Gly Pro Leu Met Phe Tyr Gly Ser Gln His Leu Thr Lys Phe 645 650 655 Ala Glu His Tyr Asn Ile Val Glu Leu Ser Met Val Ser Arg Ala His 660 665 670 Cys Leu Leu Glu Ile Lys Asn Asp Asp Leu Met His Cys Ile Ala Arg 675 680 685 Glu Ile Val Lys Arg Phe Pro Asn Val Ile Pro Thr Ala Ala Asp Ser 690 695 700 Pro Arg Val Arg Arg Ile Ser Gln Asp Ser Lys Asp Leu Glu His Val 705 710 715 720 Pro Gln Glu Ser Glu Lys Cys Leu Ile Leu Glu Ala Gly Thr Ile Asn 725 730 735 Leu Leu Trp Ile Met Gln Gly Phe Ala Ser Phe Tyr Ile Phe Asp Gly 740 745 750 Asn Ile Arg Asn Ala Ile Met Ala Ile Cys Asn Glu Met Cys Met Arg 755 760 765 Ile Val Asp Leu Thr Pro Met Leu Val Ser Asn Phe Leu His Ala Leu 770 775 780 Ala Thr Leu Arg Tyr Arg His Glu Thr Phe Leu Glu Ile Leu Val Arg 785 790 795 800 Glu Leu Glu Asp Pro Arg Leu Gly Val Lys Phe Asn Gln Asp Glu Leu 805 810 815 Lys Leu Cys Tyr Glu Ala Leu Asn Thr Phe Gly Val His Gly Pro Ile 820 825 830 Tyr Lys Val Ser Lys Met Ala Leu Lys Gln Ala His Glu Ile Asn Gly 835 840 845 Gly Asp Ser Thr Thr Thr Leu Arg Gln Val Met Ala Gly Glu Leu Lys 850 855 860 Thr Phe Gln Asp Asp Ser Glu Glu Leu Thr Gln Glu Leu Lys Ile Pro 865 870 875 880 Pro Pro Pro Lys Lys Lys Val Tyr Ile His Val Pro Glu Val Ile Arg 885 890 895 Lys His Leu Gln Val Pro Asn Ala Gln Val Thr His Gln Tyr Asp Phe 900 905 910 Val Thr Phe Gln Val 915 <210> 23 <211> 618 <212> PRT <213> babesia duncani <400> 23 Met Asp Val Phe Ser Ile Leu Leu Val Phe Ser Ala Phe Tyr Val Asn 1 5 10 15 Ala Ile Ala Ala Asp Asp Val Lys Thr Phe Leu Phe Lys Lys Asp Val 20 25 30 Glu Ser Thr Val Glu Ile Asp Ala Asn Asp Asp Ala Val Leu Val Cys 35 40 45 Pro Ile Ala Ser Val Leu Ile Ile Lys Lys Ala Arg Trp Leu Pro Val 50 55 60 Thr Gly Gly Asp Met Arg Val Lys Asp Gly Phe Ser Arg Thr Thr Arg 65 70 75 80 Ile Gly Trp Leu Cys Asn Gly Leu Glu Asn Cys Ala Phe Arg Pro Val 85 90 95 Ala His Leu Ser Lys Ile Gly Asp Arg Tyr Glu Phe Leu Gly Gln Pro 100 105 110 Ile Glu Thr Asp Ile Tyr Lys Leu Thr Val Thr Ala Thr Cys Gly Asn 115 120 125 Phe Met Phe Lys Arg Pro Gly Arg Arg Glu Met Leu Cys Ile Pro Thr 130 135 140 Ser Ala Lys Pro Asp Ile Val Leu Gly Cys Lys Asp Asn Glu Ala Ile 145 150 155 160 Glu Leu Ser Tyr Val Arg Val Gly Gly Lys Ser Lys His Gln Trp Arg 165 170 175 His Arg Asp Tyr Cys Ala Glu Ser Ile Ile Lys Thr Ala His Pro Leu 180 185 190 Cys Thr Gly Lys Lys Thr Cys Lys Ile Ala His Asp Val Phe Leu Lys 195 200 205 Asn Ala Lys Glu Cys Ile Pro Arg Glu Phe Asn Val Glu Tyr Tyr Cys 210 215 220 Ala Ala Pro His Lys Asn Ser Phe Tyr Asp Pro Leu Asp Ala Val Val 225 230 235 240 Val Asp Gly Val Ser Val Ala Thr Lys Tyr Val Leu Thr Ala Glu Asp 245 250 255 Gly Ala Arg Ala Ser Ala Lys Thr Asn Ala Tyr Gln Val Leu Gln Val 260 265 270 Asp Ser Ala Leu Trp Glu Ser Asp Gly Ala Thr Glu Arg Arg Asp Arg 275 280 285 Leu Glu Leu Val Lys Phe Leu Cys Asp Gly Arg Ala Glu Cys Val Phe 290 295 300 Ser Pro Thr Arg Ser Ile Ile Gly Pro Asp Glu Arg Lys Cys Asn Asp 305 310 315 320 Val Val Phe Gly Gly Met Val Lys Asp Thr Met Ser His Phe Met Leu 325 330 335 Arg Ala His Phe Ser Leu Val Pro Phe Asp Pro Lys Lys Tyr Asp Glu 340 345 350 Lys Glu Tyr His His Val Thr Ile Lys Ser Thr Glu Lys Lys Thr Leu 355 360 365 Glu Cys Pro Val Asn Met Ser Leu Thr Phe Tyr Val Ala Leu Trp Gly 370 375 380 Gly Lys Ile Thr Asp Thr Ser Pro Leu Lys Gly Pro Lys His Phe Val 385 390 395 400 Glu Val Asp Ile Asn Gly Glu Lys His Arg Tyr Ser Glu Ile Ile Asn 405 410 415 Ile Val Gly Thr Gln Cys Phe Gly Lys Ser Lys Cys Glu Ile Glu Pro 420 425 430 Leu Lys Leu Lys Pro Pro Arg His Glu Lys Asp Leu Lys Glu Phe Pro 435 440 445 Thr His Glu Gly Val Lys Lys Asp Asp His Gln Leu Glu Leu Tyr Tyr 450 455 460 Lys Cys Ile Asp Leu Gln Thr Leu Pro Ser Leu Val Glu Ser Leu Ile 465 470 475 480 Ser Asp Gly Pro Arg Tyr Pro Arg Glu Phe Ile Thr Pro Ile Gln Leu 485 490 495 Ser Pro Asp Met Arg Ile Val Val Met Leu Asp Ile Tyr Gly Pro Thr 500 505 510 Val Leu Glu Val Ala Asn Ala Leu Lys Leu Glu Ile Pro Val Ala Arg 515 520 525 Thr Asn Glu Ile Lys Ile Ser Trp Lys Asp Ala Lys Ile Ser Gln Gly 530 535 540 Ile Arg Leu Val Lys Asp Thr Arg Asn Tyr Val Phe Glu Phe Val Ile 545 550 555 560 Gly Ala Glu Asp Tyr Ile His Met Thr Val Asn Ser Phe Asp Asn Asp 565 570 575 Gly Ser Pro Met Ser Ile Pro Val Glu Phe Glu Ala Ser Lys Arg Ile 580 585 590 Leu Asp Phe Ser Arg Gly Ile Glu Asp Phe Val Val Ala Thr Gly Glu 595 600 605 Ile Thr Asn Phe Arg Ala Phe Ile Lys Ser 610 615 <210> 24 <211> 274 <212> PRT <213> babesia duncani <400> 24 Met Val Thr Arg Glu Met Tyr Ile Met Gly Tyr Ala Asn Val Ile Ser 1 5 10 15 Path Asp Ile Lys Lys Phe Lys Glu Thr Leu Path Asn Glu Ile Thr Thr 20 25 30 Arg Glu Glu Tyr Glu Lys Leu Lys Path Asp Ile Path Ser Thr Arg Path 35 40 45 Ile Met Gly Asp Leu Lys Ser Asn Val Arg Val Leu Thr Arg Leu Leu 50 55 60 Asn Glu Val Tyr Ile Leu Lys Thr Leu Met Arg Glu Glu Asp Val Arg 65 70 75 80 Path Leu Gly Asp Leu Ser Met Glu Path Lys Thr Leu Val Path Gly Lys 85 90 95 Lys Glu Leu Gln To Lys Leu Glu Asn Glu To Arg Glu To Lys Lys 100 105 110 Lys Val Asp Gly Leu Pro Leu Thr Lys Lys Ile Leu Glu Glu Asn Thr 115 120 125 Glu Gln Leu Leu Glu Glu Ile Ser Lys Ile Glu Met His Val Lys Lys 130 135 140 Ser Ala Glu Ala Ile Glu Lys Asn Ile Asp Glu Cys Asn Asp Lys Ile 145 150 155 160 Thr Gln Thr Asn Val Met Ala Glu Glu Glu His Glu Ala Leu Thr Asn 165 170 175 Lys Leu Gly Ile Thr Lys Ile Val Leu Asn Gly Ile Lys Thr Gly Leu 180 185 190 Leu Lys Leu Ile Ser Ile Ser Asn Arg Leu Lys Ala Ala Thr Ser Gly 195 200 205 Ala Thr Arg Glu Glu Asn Lys Ile Leu Lys Glu Thr Ile Leu Asn Arg 210 215 220 Ile Lys Phe Ile Leu Ala Glu Gly Asp Val Val Phe Lys Arg Leu Glu 225 230 235 240 Lys Asp Met Thr Asp Ile Glu Lys Arg Ile Lys Arg Ile Pro Ile Glu 245 250 255 Gly Thr Leu Pro Asp Leu Asn Thr His Gly Gly Tyr Gly Thr Ile Glu 260 265 270 Thr His <210> 25 <211> 498 <212> PRT <213> babesia duncani <400> 25 Met Asp Phe Leu Trp Leu Leu Gly Phe Ala Ile Ile Tyr Arg Lys Phe 1 5 10 15 Val Val Gly Val Gly Pro Asp Glu Asp Ser Asp Tyr Pro Glu Val Asp 20 25 30 Val Lys Ser Ser Lys Val Asn Ile Gly Ile Ser Ala Thr Val Asp Lys 35 40 45 Phe Phe Asp Asp Met Lys Leu Met Glu Glu Asp Tyr Lys Ala Tyr Gln 50 55 60 Asp Lys Ile Leu Gly Ala Leu Asn Thr Val Arg Arg Arg Leu Glu Lys 65 70 75 80 Ala Lys His Leu Glu Ala Thr Asp Leu Ser Asp Leu Ala Asn Ile Met 85 90 95 Leu Asp Val Asn Lys Glu Leu Thr Lys Met Asn Ser Cys Val Ser Arg 100 105 110 Leu Ala Ala Leu Arg Pro Tyr Val Glu Lys Ser Ile Asn Leu Leu His 115 120 125 Glu Asp Asp Lys Glu Thr Ala Lys Lys Arg Leu Leu Asn Phe Met Asn 130 135 140 Pro Asp Glu Met Val Asn Val Leu His Met Leu Phe Ser Glu Tyr Lys 145 150 155 160 Glu Leu Asn Val Glu Leu Val His Val Lys Lys Arg Gly Thr Ala Pro 165 170 175 Ser Gln Ser Glu Ser Leu Ser Lys Ser Lys Ile Glu Ser Leu Ser 180 185 190 Ser Leu Ser Ala Leu Asn Gln Glu Pro Gly Arg Ile Leu Glu Pro Ala 195 200 205 Leu Ala Ile Tyr Asp Lys Ile Met Asn Gly Gly Thr Glu Ile Leu Glu 210 215 220 Glu Met Asn Lys Leu Asn Leu Lys Ile Gln Gly Lys Gln Thr Met Ser 225 230 235 240 Ser Met Glu Tyr Leu Tyr Ile Val Gln Asn Met Leu His Ala Lys Glu 245 250 255 Tyr Val Met Glu Ser Lys Gln Pro Leu Thr Ser Leu Gly Tyr Leu Gly 260 265 270 Thr Ala Leu Asp Gln Met Gln Phe Thr Tyr Ser Pro Thr Glu Lys Ser 275 280 285 His Val Glu Asn Ile Lys Lys Glu Val Gly Glu Ile Leu Asn Gly Ile 290 295 300 Lys Asp Phe Gln Asn Lys Val Lys Asn Ser Ile Asp Thr Val Glu Lys 305 310 315 320 Arg Val Thr Thr Ile Ser Val Thr Asp Ala Leu Pro Lys Glu Arg Ala 325 330 335 Leu Glu Ile Ile Ser Ala Val Pro Ala Tyr Val Gln Ile Phe Lys Lys 340 345 350 Gln Met Asp Leu Glu Lys Gly Ala Val Leu Asn Asp Ile Asn Glu Leu 355 360 365 Asp Lys Gln Leu Asp Glu Lys Lys Arg Ile Pro Ser Lys Glu His Glu 370 375 380 Gln Met Glu Ala Lys Ile Pro Ile Leu Glu Thr Gln Val Gln Phe Phe 385 390 395 400 Leu Glu Phe Ile Glu Ala Met Lys Tyr Phe Arg Val Thr Cys Glu Met 405 410 415 Ile Pro Lys Met Met Gly Val Asp Glu Lys Lys Gln Phe Arg Arg Glu 420 425 430 Leu With Leu Cys Asp Met With Leu Lys Asn Glu Lys Gln Glu Tyr Asp 435 440 445 Phe Met With Glu Gln Phe Lys Lys Val Lys Glu Arg With Val Gln Thr 450 455 460 Arg Pro Arg Ala Ser Arg Phe Lys Arg Lys His Ser Gly Phe Ser Thr 465 470 475 480 Met Glu Pro To Be A Leopard Leopard Val Leopard Pro Val Ile Val To Be A Leopard 485,490,495 Where Tyr <210> 26 <211> 414 <212> PRT <213> babesia duncani <400> 26 Met Gly Asn Ala Cys Cys Lys Ser Ser Pro Pro Ala Ala Val Ser Asp 1 5 10 15 Ala Lys Thr Ala Asp Lys Pro Asn Phe Glu Ser Leu Ser Thr Leu Ser 20 25 30 Met Lys Asn Asp Gly Ser His Arg Asn Gln Glu Lys Ala Pro Ser Ala 35 40 45 Lys Ala Ser Pro Arg Lys Asn Val Glu Phe Lys Phe Thr Asp Thr Gly 50 55 60 Tyr Asp Ala Thr Gly Ala Lys Lys Trp Asp Glu Lys Val Ile Ser Ala 65 70 75 80 Leu Leu Gly Gly Lys Pro Thr Asn Ile Glu Ala Ala Pro Gly Ile Asp 85 90 95 Val Gly Asp Gly Leu Val Glu Arg Gly Pro Val Leu Leu Lys Asp Gly 100 105 110 Ser Val Tyr Cys Gly Gln Trp Lys Gly Ser Val Arg His Gly Arg Gly 115 120 125 Gln Phe Phe Asp Val Asp Gly Thr Gln Tyr Ile Gly Asn Phe Ser Lys 130 135 140 Gly Val Phe Glu Gly Ala Gly Glu Leu Arg Thr Trp Thr Gly Asp Lys 145 150 155 160 Tyr Gln Gly Leu Phe Lys Asn Gly Lys Tyr His Gly Lys Gly Ile Phe 165 170 175 Thr Gln Lys Asn Gly Asp Val Tyr Glu Gly Val Phe Val Asp Gly Met 180 185 190 Arg Glu Gly Tyr Gly Thr Glu Arg Tyr Lys Asp Gly Ser Val Tyr Met 195 200 205 Gly Glu Phe Lys Gly Gly Lys Arg Met Gly Asn Gly Glu Leu Lys Met 210 215 220 Ala Asp Gly Val Leu Tyr Glu Gly Glu Phe Asn Asp Glu Ile Thr Gly 225 230 235 240 Lys Gly Lys Met Phe Trp Pro Thr Gly Glu Cys Tyr Val Gly Ser Phe 245 250 255 Leu Lys Gly Met Lys His Gly Leu Gly Glu Thr Thr Trp Lys Thr Gly 260 265 270 Pro Met Lys Ser Gln Arg Gly Lys Tyr Glu Asn Gly Lys Met Cys Gly 275 280 285 Thr Phe Glu Asn Val Met Arg Asp Gly Lys Val Val Lys Gly Val Tyr 290 295 300 Lys Asp Gly Ile Leu Leu Gln Glu Ile Thr Asp Thr Lys Pro Lys Val 305 310 315 320 Ala Pro Val Val Thr Gln Pro Pro Pro Val Lys Glu Gln Ala Thr Pro 325 330 335 Thr Pro Thr Pro Lys Ala Ala Ala Ser Pro Thr Thr Ser Thr Pro Thr 340 345 350 Arg Ala Ala Ala Ser Ala Ser Pro Thr Leu Ser Arg Ala Pro Ser Thr 355 360 365 Ser Ser Thr Pro Ala Thr Ala Thr Pro Pro Ala Ser Thr Pro Thr Ala 370 375 380 Ala Ala Ser Thr Gln Ala Lys Pro Lys Ala Lys Ser Ala Lys Ser Ser 385 390 395 400 Ser Ala Ala Lys Lys Lys Thr Ser Ser Lys Ser Ser Ala Arg 405 410 <210> 27 <211> 376 <212> PRT <213> babesia duncani <400> 27 Met Ala Asp Glu Glu Val Thr Ala Leu Val Ile Asp Asn Gly Ser Gly 1 5 10 15 Asn Val Lys Ala Gly Val Ala Gly Asp Asp Ala Pro Arg Cys Val Phe 20 25 30 Pro Ser Ile Val Gly Arg Pro Lys Asn Pro Ala Leu Met Val Gly Met 35 40 45 Asp Glu Lys Asp Thr Tyr Val Gly Asp Glu Ala Gln Ser Lys Arg Gly 50 55 60 Ile Leu Thr Leu Lys Tyr Pro Ile Glu His Gly Ile Val Thr Asn Trp 65 70 75 80 Glu Asp Met Glu Lys Ile Trp His His Thr Phe Tyr Asn Glu Leu Arg 85 90 95 Met Ala Pro Glu Glu His Pro Val Leu Leu Thr Glu Ala Pro Met Asn 100 105 110 Pro Lys Ala Asn Arg Glu Lys Met Thr Thr Ile Met Phe Glu Thr His 115 120 125 Asn Val Pro Ala Met Tyr Val Ala Ile Gln Ala Val Leu Ser Leu Tyr 130 135 140 Ser Ser Gly Arg Thr Thr Gly Ile Val Leu Asp Ser Gly Asp Gly Val 145 150 155 160 Thr His Thr Val Pro Ile Tyr Glu Gly Tyr Ala Leu Pro His Ala Met 165 170 175 Met Arg Leu Asp Leu Ala Gly Arg Asp Leu Thr Asp Phe Met Gln Lys 180 185 190 Ile Leu Ala Glu Arg Gly Phe Ser Phe Thr Thr Thr Ala Glu Arg Glu 195 200 205 Ile Val Arg Asp Ile Lys Glu Lys Leu Cys Tyr Val Ala Leu Asp Phe 210 215 220 Glu Glu Glu Met Thr Asn Ala Glu Ser Ser Ser Glu Ile Glu Lys Ser 225 230 235 240 Tyr Glu Leu Pro Asp Gly Asn Ile Ile Thr Val Gly Asn Glu Arg Phe 245 250 255 Arg Cys Pro Glu Val Leu Phe Gln Pro Ser Phe Ile Gly Met Glu Ala 260 265 270 Ala Gly Ile His Thr Thr Thr Phe Lys Ser Ile Thr Lys Cys Asp Val 275 280 285 Asp Ile Arg Lys Asp Leu Tyr Ala Asn Val Val Leu Ser Gly Gly Thr 290 295 300 Thr Met Tyr Glu Gly Ile Gly Gln Arg Met Thr Lys Glu Leu Asn Ala 305 310 315 320 Leu Val Pro Ser Thr Met Lys Ile Lys Val Val Ala Pro Pro Glu Arg 325 330 335 Lys Tyr Ser Val Trp Ile Gly Gly Ser Ile Leu Ser Ser Leu Ser Thr 340 345 350 Phe Gln Gln Met Trp Ile Thr Lys Glu Glu Phe Asp Glu Ser Gly Pro 355 360 365 Asn Ile Val His Arg Lys Cys Phe 370 375 <210> 28 <211> 292 <212> PRT <213> babesia duncani <400> 28 Met Ala Ile Trp Lys Leu Phe Val Phe Gly Ile Cys Gly Ala Gly Lys 1 5 10 15 Val Leu Gly Tyr Arg Leu Asp Asp Val Leu Gln Gly Asp Gly Glu Asp 20 25 30 Phe Ala Leu Phe Gly Leu Gly Lys Glu Val Ile Glu Ala Arg Met Asp 35 40 45 Lys Leu Phe Ser Val Ile Asp Leu Asn Asn Asp Gly Ile Leu Asp Leu 50 55 60 Glu Glu Leu Ala Ala Phe His Ala Lys Thr Phe Gln Thr Ile Leu Asp 65 70 75 80 Leu Gln Leu Asn His Glu Met Glu Leu Val Asp Arg Asn Lys Asp Gly 85 90 95 Phe Val Asp Val Glu Glu Leu Lys Val Ala Phe Glu Arg Glu Gly Thr 100 105 110 Gln Asp Val Asp Ile Ser Thr Val Glu Lys Gly Leu Gln Arg Arg Phe 115 120 125 Val Ala Ala Asp Lys Asp Gln Asp Gly Lys Leu Asn Arg Gln Glu Leu 130 135 140 Gly Leu Leu Leu Asn Pro Gly Arg Asp Glu Glu Leu Ile Asn Ile Glu 145 150 155 160 Ile Glu Glu Ile Met Gln Thr Tyr Asp Gln Asn Gly Asp Gly Leu Val 165 170 175 Ser Leu Glu Glu Tyr Ser His Gly Arg Ser Asp Gln Glu Gly Val Ser 180 185 190 Ala Glu Phe Lys Pro Phe Asp Ser Asn Ala Asp Gly Phe Leu Ser Arg 195 200 205 Glu Glu Ile Arg Gly Val Tyr Val Glu Glu Asn Lys Asn Asp Leu Asp 210 215 220 Ser Glu His Glu Asp Leu Phe Ala Ile Thr Gly Lys Lys Pro Ile Thr 225 230 235 240 Arg Glu Val Trp Asn Ala Asn Leu Asn Lys Ile Ala His Thr Ser Leu 245 250 255 Thr Asp His Gly Glu Met Leu Arg Phe Pro Glu Asp Tyr His Met Asp 260 265 270 Leu Gly Asp Ile Pro Arg Asp Arg Lys Asp Gly Ala Glu Glu Arg Pro 275 280 285 Ser Gly Liver Glu 290 <210> 29 <211> 476 <212> PRT <213> babesia dunkin <400> 29 Met Cys Gly Asn Gly Ile Ile Asn Asn Leu Val Tyr Leu Lys Met Asp 1 5 10 15 Ser Ile Arg Glu Ser Thr Ser Phe His Asn Asp Phe Tyr Tyr Ile Thr 20 25 30 Cys Pro Phe Ser Ile Lys Gly Phe Leu Lys Glu Tyr Trp Leu Ser Thr 35 40 45 Ile Thr Phe Phe Leu Thr Phe Ala Ala Val Phe Ile Pro Ser Val Phe 50 55 60 Lys Leu Asp Leu Lys Asp His Ala Asp Tyr Val Met Leu Pro Ala Asn 65 70 75 80 Met Phe Leu Arg His Ile Arg Gly Phe Val Val Leu Phe Met Phe Phe 85 90 95 Ala Ser Ala Ala Lys Ile Arg Leu Phe Leu Gln Arg Lys Val Asp Ser 100 105 110 Leu Lys Thr Arg Ile Met Ile Lys Tyr Leu Ile Ala Gly Leu Leu Ser 115 120 125 Leu Leu Val Thr Leu Gly Leu Ala Ala Leu Ile Ile Pro Leu Asn Thr 130 135 140 Ser Leu Gly Gly Asn Thr Tyr Phe Ser Pro His Ser Ile Lys Asp Tyr 145 150 155 160 Asn Pro Thr Thr Glu Phe Lys Asn Phe Ile Asn His Leu Ala Val His 165 170 175 Asp Leu Pro Leu Asn Met Ala Thr Thr Arg Val Asp Phe Val Asn Glu 180 185 190 Phe Gly Lys Asp Gln Leu His Glu Gly Leu Gly Asp Gly Tyr Asn Ala 195 200 205 Pro Gly Phe Val Val Tyr Gly Leu Leu Phe Ala Phe Ala Ile Tyr Thr 210 215 220 Met Asp Glu His Thr Asp Ala Leu Cys Asn Ile Ile Thr Ala Met His 225 230 235 240 Lys Cys Leu Leu Ser Val Tyr Trp Ile Leu Val Val Tyr Ser Pro Phe 245 250 255 Ala Phe Phe Leu Ala Gly Leu Val Thr Phe Asp Glu Leu Lys Val Lys 260 265 270 Gly Gly Leu Gly Ile Ala Leu Met Gly Tyr Leu Tyr Leu Thr Leu Ala 275 280 285 Val Leu Ala Val Phe Val Ala Trp Ser Phe Ile Val Val Pro Leu Leu 290 295 300 His Phe Ile Arg Thr Ala Arg Asn Pro Tyr Pro Thr Ile Ile Lys Leu 305 310 315 320 Leu Pro Tyr Leu Pro Thr Ala Phe Cys Ser Gly Ser Ser Val Leu Ser 325 330 335 Gly Glu Lys Thr Lys Asp Phe Leu Lys Lys Arg Gly Phe Asp Pro Asp 340 345 350 Asp Val Glu Asn Tyr Leu Thr Phe Ser Thr Leu Val Asn Phe Ser Gly 355 360 365 Thr Thr Ser Gly Phe Thr Val Cys Ala Ile Leu Met Leu Lys Leu Phe 370 375 380 Gly Lys Ser Leu Asp Trp Val Thr Val Leu Lys Ile Ile Val Thr Gly 385 390 395 400 Leu Leu Val Gly Phe Thr Ile Val Glu Tyr Ile Gln Gly Tyr Leu Phe 405 410 415 Gly Ile Ile Phe Phe Leu Asn Asn Thr Met Leu Pro Pro Gly Ser Ile 420 425 430 Ile Leu Leu Leu Gln Ile Asp Trp Leu Leu Asp Arg Phe Arg Ile Val 435 440 445 Ser Asn Val Ile Asp Asp Ala Leu Thr Ile Asp Glu Ile Thr Asn Val 450 455 460 Lys Ser Lys Leu Ser Ser Cys Pro Phe His Lys Val 465 470 475 <210> 30 <211> 967 <212> PRT <213> babesia duncani <400> 30 Met Gly Glu Gly Thr Asn Lys Thr Gln Tyr Pro Phe Ile Leu Gly Leu 1 5 10 15 His Glu Glu Val Val Cys Ala Ala Lys Arg Leu Glu Ile Cys Leu Leu 20 25 30 Glu Lys Ile Glu Gln Leu Gly His Val Asp Asp Lys Gly Trp Lys Val 35 40 45 Cys Val Asp Ser Thr Ile Glu Gly Lys Leu Leu Gly Asn His Ile Thr 50 55 60 Cys Leu Ser Leu Cys Lys Val Pro Asn Gly Ser His Gly Ser Glu Phe 65 70 75 80 Leu Leu Ala Val Gly Tyr Lys Ser Gly Leu Ile Ala Leu Ala Arg Val 85 90 95 Asp Ser Gln Asn Glu Phe His Ile Leu Ser His Asn Asp Gln Asn Lys 100 105 110 Ser Ser Ile Ser Gln Ile Glu Leu Lys Tyr Val Gly Glu Ser Thr Ala 115 120 125 Ala Tyr Asn Leu Met Ser Leu Arg Val Tyr Ala Phe Leu Asp Ser Gly 130 135 140 Lys Ile Ile Thr Phe Ser Trp Gly Asp Lys Ile Gln Thr Ser Ile Gln 145 150 155 160 Ser Gly Glu His Val Leu Gly Phe Ala Val Asn Ser Gln Asn Thr Thr 165 170 175 Ile Ala Ile Leu Gln Asn Thr Gly Ile Val Cys Arg Ser Leu Asp Thr 180 185 190 Glu Thr Ile Leu Arg Thr Leu Glu Asn Val Gln Ile Val Asn Ala Asn 195 200 205 Arg His Tyr Leu Ser Trp His Pro Tyr Lys Asn Leu Leu Val Phe Leu 210 215 220 Asp Asn Lys Gly Ile Ser Tyr Thr Cys His Pro Lys Trp Asp Val Tyr 225 230 235 240 Lys Phe Ser Gln Asn Ser Gln His Gln Glu Leu Ile Arg His Val Gln 245 250 255 Phe Gly Ile Cys Gly Asp Phe Val Leu Leu Leu Thr Ala Ser Phe Asp 260 265 270 Lys Ile Ile Ile Trp Asp Phe Glu Thr Glu Ser Ile Leu Tyr Ser His 275 280 285 Lys Gly Cys Asp Met Val Ala Cys Gly Leu Ile His Leu Ser Asn Lys 290 295 300 Arg Val Arg Leu Ala Val Phe Ala Asn Phe Ala Ser Asn Glu Phe Trp 305 310 315 320 Arg Cys Lys Arg Leu Ile Met Ser Gly Asp Glu Leu Met Glu Glu Ala 325 330 335 Lys Ser Glu Leu Pro Gln Ser His Lys Thr Arg Arg Leu Lys Arg His 340 345 350 Ile Thr Glu Leu Asp Asp Tyr His Ile Arg Lys Met Val Asp Gln Glu 355 360 365 Ala Val Asp Glu Asp Asn Glu Glu Gln Asp Glu Glu Tyr Lys Asp Glu 370 375 380 Glu Thr Tyr Arg Asp Ile Leu Asp Ser Tyr Asp Asn Leu Asp Lys Asp 385 390 395 400 Glu Met Thr His Phe Asp Gln Ser Arg Val His Val Met His Glu Ile 405 410 415 Ser Lys Leu Arg Lys Lys Val Ala Ser Leu Asp Asn Arg Val Ala Glu 420 425 430 Arg Thr Thr Leu Val Pro Gly Ser Cys Pro Ala Pro Asp Asp Ala Ala 435 440 445 Val Gln Trp Val Leu Phe Trp Asp Glu Val Gly Gln Ile Thr Lys Gln 450 455 460 Leu Ile Ser Asp Val Trp Cys Leu His Val His Val Phe Ser Gly Pro 465 470 475 480 Leu Ala Gly Tyr Lys Arg Lys Pro Asp Arg Tyr Asn Cys His Thr Ala 485 490 495 Ala Leu Asn Gln Lys Tyr Val Val Thr Gly Ser Glu Ile Asn Val Asp 500 505 510 Gly Gly His Val His Gly Ile Leu Thr Phe Leu Asp Phe Glu Asn Asn 515 520 525 Thr Gln Trp Asp Arg Arg Phe Phe Asn Glu Tyr Ile Ser Ala Val Ala 530 535 540 Val Gly Asp Ser Phe Val Ala Ala Ile Thr Ala Asp Gly Ile Leu Tyr 545 550 555 560 Ile Leu Ser Leu Ala Arg Ser Leu Met Gly Val Phe Gln Leu Lys Gly 565 570 575 Ser Pro Ile Ala Ile Ala Ala Arg Gly Asn Val Leu Ala Thr Ile Thr 580 585 590 Glu Ala Thr Thr Leu Thr Asn Val Ser Ser Phe Gly His Val Arg Met 595 600 605 Phe Trp Val Asn Gly Leu Arg Gly Leu Ala Lys Asn Pro Ala Ser Arg 610 615 620 Ile Val Asp Leu Tyr Ser Asp Ser Leu Val Leu Gly Pro Asp Lys Ala 625 630 635 640 Ile Ser Trp Ile Ser Phe Ser Ser Gln Cys Thr Leu Trp Ile Thr Asp 645 650 655 Thr Ser Gly Gln Leu Met Ala Leu Leu Pro Ala Ile Glu Ser Cys Tyr 660 665 670 Lys Val Gly Gly Tyr Ser Leu Glu Trp Ile Pro Phe Met Asn Leu Glu 675 680 685 Asn Leu Val Asn Glu Ser Ser Asp Tyr Glu Pro Ser His Thr Val Phe 690 695 700 Pro Leu Tyr Val Ser Asp Met Lys Leu Asn Tyr Ile Leu Leu Lys Arg 705 710 715 720 Gly Gln Ser Tyr Pro Thr Cys Ser Gln Pro Leu Asn Phe Met Gly Tyr 725 730 735 Thr Leu Lys Lys Ala Cys Leu Arg Ile Asp Gly Cys Val Gly Ala Tyr 740 745 750 Leu Pro Phe Gln Lys Phe Asn Gly Leu Val Thr Lys Asp Pro Gln Leu 755 760 765 Arg Glu Val Ile Gly Ser Asp Ile Ile Ser Asp Val Ala Ser Ile Pro 770 775 780 Trp Gln Gln Tyr Asp Glu Met Arg His Ile Gln Ser Leu Gln Ala Cys 785 790 795 800 Gln Asn Glu Tyr Ile Leu Lys Val Phe Gln Asn Tyr Asn Phe Trp Met 805 810 815 Gln Asn Ser Gln Gly Ile Ser Asp Asp Ala Ile Ser Ala Phe Gly Asn 820 825 830 Ala Glu Arg Val His Asp Lys Trp Thr Leu Arg Ile Leu Arg Lys Thr 835 840 845 Lys Asp Ser Lys Gln Asp Ser Gly Val Leu Leu Asp Ala Leu Trp Met 850 855 860 Leu Arg Phe Pro Lys Cys Leu Glu Ala Ala Phe Ser Ile Leu Gln Asn 865 870 875 880 Gln Leu Asp Ala Lys Gln Arg Gln Val Leu Gln Glu Ala Ser Leu Leu 885 890 895 Leu Glu Asn Val Thr Pro Phe Glu Asn Asn Val Gln Pro Leu Asp Ala 900 905 910 Gln Ser Gln Pro Thr Ala Thr Val Ser Ile Pro Lys Gln Asp Leu Asp 915 920 925 Pro Ile Pro Lys Lys His Ala Pro Leu Ile Gln Gly Pro Ser Asn Arg 930 935 940 Leu Gln Glu Phe Val Pro Leu Gly Asn Glu Pro Glu Glu Ser Gly Pro 945 950 955 960 Leu Phe Lys Asn Ile Leu Glu 965 <210> 31 <211> 401 <212> PRT <213> Babesia duncani <400> 31 Met Val Asp Phe Glu Pro Glu Ser Cys Arg Lys His Val Asp Lys Asn 1 5 10 15 Thr Arg Ile Tyr Val Asp Gly Ala Phe Asp Leu Leu His Trp Gly His 20 25 30 Leu Asn Ala Leu Arg Gln Ser Tyr Lys Leu Gly Gly Glu Leu Ile Val 35 40 45 Gly Ile Asn Gly Asp Val Glu Thr Phe His Ala Lys Gly Ile Ser Pro 50 55 60 Ile Tyr Asn Gln Asp Glu Arg Ala Glu Leu Val Lys Gly Cys Arg Trp 65 70 75 80 Val Asn Glu Val Met Val Gly Thr Pro Tyr Glu Val Asn Leu Asp Phe 85 90 95 Leu Val Asn Ile Ala Lys Cys Asp Tyr Ile Ala His Gly Asp Asp Ile 100 105 110 Ala Ile Gly Ala Ser Gly Lys Asp Ala Tyr Asp Glu Pro Lys Lys Ala 115 120 125 Gly Lys Phe Ile Phe Phe Arg Arg Ser Leu Gly Val Ser Thr Ser Thr 130 135 140 Thr Val Gly Arg Leu Ile Asp Ala Leu Glu Ser Asp His Phe Ser His 145 150 155 160 Leu Ser Lys Asn Ser Glu Asn Lys Leu Gln Tyr Gly Asp Phe Glu Lys 165 170 175 Ala Leu Gln Glu Asn Glu Glu Gln Met Ile Asn Glu Gly Ile Ile Asp 180 185 190 Asp Ala Leu Phe Ser Gly Asn Asn Lys His Asp Asn Lys Asn Lys Lys 195 200 205 Ser Thr Asp Val Phe Pro Tyr Pro Arg Phe Arg Leu Ser Thr Ser Leu 210 215 220 Leu Gly Glu Phe Ile Thr Pro Lys Pro Lys Pro Lys Gly Gly Lys Ile 225 230 235 240 Ile Tyr Val Asp Gly Ser Phe Asp Val Phe His Val Gly His Leu Arg 245 250 255 Leu Leu Lys Arg Ala Arg Glu Met Gly Asp Tyr Leu Ile Val Gly Ile 260 265 270 Tyr Asp Asp Gln Thr Val Arg Thr Leu Lys Gly Thr Pro Phe Pro Phe 275 280 285 Ser Ser Leu Met Asn Arg Ala Leu Thr Ile Leu Gly Met Arg Tyr Thr 290 295 300 Asp Asp Val Val Leu Gly Ala Pro Tyr Val Pro Ser Arg Thr Tyr Leu 305 310 315 320 Glu Asn Leu Gly Ile Thr Thr Val Val Thr Gly Lys Gln His Asp Ser 325 330 335 Lys Met Ile Asn Arg Asp Phe Asp Pro Tyr Arg Glu Ala Arg Asp Met 340 345 350 Asp Ile Leu Val Glu Ile Asp Ser Gly Ser Asp Ile Thr Thr Ser Asp 355 360 365 Ile Ile Ala Arg Val Ser Ser Arg Met Asp Gln Ile Thr Ala Asn Ile 370 375 380 Arg Lys Arg Cys Ala Ile Glu Lys Thr Arg Lys Asn Ile Val Cys Ser 385 390 395 400 Leu <210> 32 <211> 516 <212> PRT <213> babesia duncani <400> 32 Met Leu Asn Asn Ala Asn Thr Val Lys Glu Val Gly Phe Arg Lys Ser 1 5 10 15 Val Ile Tyr Gln Pro Asn Val Phe Lys Asp Ala Asp Gly Val Ile Lys 20 25 30 Ile Lys Thr Asn Asn Lys Asn Ile Trp Ile Arg Gln Asn Ser Lys Cys 35 40 45 Trp Glu Phe Thr Ser Lys Thr Pro Ile Thr Ser Val Asp Asp Tyr Tyr 50 55 60 Lys Glu Leu Leu Ser Asp Phe Asn Thr Asp Asp Ser Thr Ser Ile Thr 65 70 75 80 Leu Tyr Asn Ala Asn Val Asp Leu Ala Lys Arg Gly Phe Asn Asn Phe 85 90 95 His Glu Gly Tyr Thr Lys Ile Lys Lys Leu Tyr Cys Ser Ile Leu Glu 100 105 110 Ala Gly Leu Met Ile Pro Tyr Ser Gly Met Leu Ser Gly Asp Phe Met 115 120 125 Tyr Ala Val Val Ser Leu Pro Asp Lys Leu Asp Ile Thr Tyr Cys Pro 130 135 140 Ile Asp Asn Tyr Met Glu Asn Pro Thr Lys Ser Glu Cys Glu Asn Ile 145 150 155 160 Asn Arg Trp Met Glu Phe Phe Lys Met Tyr Gly Thr His Val Ser Thr 165 170 175 His Ile Ile Thr Gly Gly Lys Ile Phe His Glu Tyr Lys Thr Leu Asn 180 185 190 Ile Thr Glu Tyr Arg Lys Lys Ser Lys Phe Arg Gln Ser Thr Asn Ile 195 200 205 Phe Glu Val Thr Asn Ile Asn Phe Asp Ser Ala Gly Gln Lys Ser Thr 210 215 220 Lys Asn Thr Ile Val Phe Gly Gly Asn Tyr Val Lys Gly Met Glu Ser 225 230 235 240 Glu Ala Arg His Phe Tyr Asn Glu Trp Ser Lys Thr Leu Glu Ser Arg 245 250 255 Ser Leu Pro Ile Lys Val Thr Val Lys Pro Leu Ser Ile Phe Met Ser 260 265 270 Tyr Arg Asn Asp Ile Tyr Lys Glu Ala Leu Lys Phe Tyr Arg Asp Val 275 280 285 Ala Leu Leu Thr Thr Val Gly Ile Gln Tyr Ser Thr Lys Ile Asp Glu 290 295 300 Leu Leu Arg Glu Ser Thr Thr Val Val Ser Asp Asp Gly Met Ala His 305 310 315 320 Cys Pro Thr Asn Gln Ile Val Leu Ala Gly Phe Ile Met Ser Lys Asn 325 330 335 Pro Lys Val Pro Ile Val Asn Cys Glu Gln Gly Lys Ile Leu Cys Ser 340 345 350 Asn Gly Thr Asp Lys Pro Ala Ser Val Tyr Ile Ile Cys Val Lys Glu 355 360 365 Leu Asn Asp Ile Ile Thr Thr Ser Thr Ser Met Glu Asn Val His Ile 370 375 380 Cys Pro Asn Gly Asn Val Thr Ala Leu Gly Phe Ala Phe Arg Lys Gln 385 390 395 400 Ser Glu Ser Asp Asp Trp Thr Val Val Ile Pro Arg Ile Gly Lys Gln 405 410 415 Gln Met Ile Asn Tyr Thr Lys Gly Leu Asn Met Ser Trp Leu Leu Cys 420 425 430 Val Pro Ile Glu Ile Met Phe Trp His Met Glu Met Ile Ile Asp Ser 435 440 445 Ala Pro Lys Asp Asp Ser Arg Thr Val Ser Cys Lys Thr Gly Trp Thr 450 455 460 Ile Leu Lys Gly Phe Lys Leu Met Phe Leu Lys Lys Glu Asp Thr Thr 465 470 475 480 Arg Val Val Leu Glu Glu Cys Ile Ser His Gln Gln His Cys Ile Leu 485 490 495 Asn Cys Asn Glu Glu Cys Thr Lys Met Tyr Gly Thr Ile Leu Cys Lys 500 505 510 Lys Gln His Asp 515 <210> 33 <211> 2356 <212> PRT <213> babesia duncani <400> 33 Met Ser Thr Asn Gly Thr Val Arg Trp Arg Thr Ser Ser Arg Ser Gln 1 5 10 15 Leu Arg Asp Arg Arg Lys Asn Ala Leu Thr Arg Arg Leu Arg Phe Glu 20 25 30 Val Gly Arg Leu Asp Thr Glu Ala Phe Glu Thr Arg Thr Lys Tyr Leu 35 40 45 Arg Glu Ile Phe Leu Asp Val Asp Lys Arg Asn Ser His Asp Trp Thr 50 55 60 Ala Leu Glu Lys Lys Ile Leu Leu Leu Asp Trp Cys Gln Asn Pro Gln 65 70 75 80 Lys Phe Glu Lys Trp Lys Pro Ala Ala Thr Glu Asp Met Gln Ser Arg 85 90 95 Phe Phe Ala Asn Leu Ile Phe Asn Tyr Ser His Leu Ala Met Ile Asn 100 105 110 Ser Gly Met Cys Ile Val Ile Val Arg Leu Val Pro Leu Val Val Asn 115 120 125 Ile Lys Ala Pro Tyr Gln Cys Val Ile Leu Leu Val Arg Asp Asn Val 130 135 140 Asn Gly Met Val Ile Asp Arg Leu Lys Val Gly Leu Ile Trp Arg Gly 145 150 155 160 Lys Asp Thr Asn Thr Asp Val Leu Gly Lys Ser Thr Arg Ile Phe Thr 165 170 175 Pro Pro Leu Ser Thr Asp Phe Gln Phe Leu Ser His Gly Ile Gly Tyr 180 185 190 Asn Phe Lys Ser Leu Leu Pro Gln Thr Glu Phe Glu Pro His Val Ala 195 200 205 Cys Ser Asp Cys Ile Ser Arg Glu Leu Glu Ser Leu Cys Thr Leu Glu 210 215 220 Thr Pro Asp Ile Val Leu Glu Ser Pro Ala Leu Gly Met Glu Val Thr 225 230 235 240 Ser Ser Phe Val Asn Gly His Lys Val Tyr Leu Val Val Thr Arg Gly 245 250 255 Val Asp Gly Ile Val Arg Ile His Arg Val Gln Glu Leu Ile Gln Thr 260 265 270 Ser Ile Asp Ile Ile Arg Thr Trp Glu Gln Leu Arg Leu Lys His Leu 275 280 285 Lys Arg Thr Met Gln Ser Gln Gln Tyr Ala Ala Cys Thr Gly Cys Leu 290 295 300 Val His Lys Glu Glu Leu Gln Gln Leu Tyr His Leu Lys Gln Cys Ala 305 310 315 320 Arg Ser Phe Ala Pro Glu Cys Gly Pro Met Gln Phe Val Gly Leu Glu 325 330 335 Met Ile Asp Val Ala Arg Pro Arg Thr Cys Ala Thr Lys Arg Glu Ala 340 345 350 Cys Gly Leu Pro Leu Ala Leu Gly Tyr Thr Ser Val Arg Asn Glu Gln 355 360 365 Ala Val Ile Pro Ser Leu Leu Met Ala Met Ala Ser Asn Thr Val Cys 370 375 380 Ile Trp Ser Ile Tyr Ser Tyr Leu Lys Glu Trp Asn Leu Asn Pro Leu 385 390 395 400 Gly Pro Ile Lys Val Met Thr Tyr Pro Asp Gly Thr Leu Pro Thr Asp 405 410 415 Ile Ser Ser Thr Val Ser Ile Ala Ala Ser Leu Glu Ala Leu Glu Arg 420 425 430 Leu Glu Phe Ile His Ala Pro Lys Phe Tyr Thr Thr Asp Asp Arg Gly 435 440 445 His Leu Ser Leu Trp Ser Leu Gly Ser Thr Gly Pro Glu Ala Gln Val 450 455 460 Thr Leu Asp Gln Asn Ala Leu Cys Ser Cys Ala Val Asn Arg Ser Tyr 465 470 475 480 Pro His Ile Val Ala Val Gly Leu Asp Val Gly Lys Ile Lys Ile Tyr 485 490 495 Asn Thr Leu Thr Gln Gly Thr Thr Cys Ile Ala Gln Met Glu His Pro 500 505 510 Leu Leu Thr Lys Val Gln Thr Leu Gln Ser Phe Leu Pro Asp Asn Val 515 520 525 Tyr Asp Tyr Gln Arg Trp Tyr His Pro Val Val Lys Leu Glu Trp Ile 530 535 540 Ser Asp Val Phe Ile Leu Ala Gln Tyr Ser Glu Pro Ile Phe Thr Thr 545 550 555 560 Glu Ser Thr Asn Ala Ser Ala Val Ala Ile Trp Asn Val Val Lys Asp 565 570 575 Ile Phe Asp Arg Asp Asp Ala Leu Val Cys Asn Lys His Trp Ser Leu 580 585 590 Asn Ser Cys Asn Leu Tyr Asn Thr Trp His Leu Ala Ser Lys Leu Val 595 600 605 Cys Leu Tyr Gly Gly His Phe Gly Cys Ile Cys Gly Val Leu Ser Ser 610 615 620 Asp Ala Lys Trp Ser Ala Glu Gln Gly Leu Leu Ala Val Thr Ile Asp 625 630 635 640 Ser Thr Gly Gln Leu His Val Phe Lys Pro Gly Ile Trp Thr Trp Gly 645 650 655 Asp Cys Asp Asp Pro Met Ala Ile Ala Arg Leu Thr Gly Asp Cys Glu 660 665 670 Phe Tyr His Ser Ile Leu Ala Arg Val Gln Glu Gln His Arg Arg Leu 675 680 685 Ser Val Pro Val Met Glu Ile Asp Asn Ser Val Asp Met Gly Gln Gly 690 695 700 Thr Arg Leu Arg Lys Thr Arg Ala Lys Phe Ser Thr Tyr Ile Gln Asp 705 710 715 720 Ala Gln Thr Gln Leu Glu Ser Val Glu Thr Ala Ser Gly Leu Glu Glu 725 730 735 Ile Asn Ser Leu Glu Lys Leu Pro Met Phe Cys Lys Lys Thr Leu Arg 740 745 750 Leu Asn Ser Glu Ser Glu Lys Tyr Leu Lys Leu Val His Arg Leu Val 755 760 765 Ala Glu Arg Glu His Ala Glu Phe Leu Leu Ser Gln Gly Thr Pro Gly 770 775 780 Lys Thr Gly Lys Arg Lys Cys Pro Leu Gly Ala Pro Asn Ile Lys Gln 785 790 795 800 Glu Pro Leu Glu Leu Ile Glu Ala Pro Gln Gly Pro Ser Ser Glu Ala 805 810 815 Pro Val Lys Ser Lys Asn Glu Tyr Gln Asn Asp Ala Met Glu Pro Glu 820 825 830 Ser Phe Asn Phe Ser Ser Val Leu Thr Lys Phe Asp Thr Asp Val Ser 835 840 845 Met Glu Pro Glu Thr Glu Leu Val Glu Thr Ala Leu Pro Val Val Gln 850 855 860 Pro Thr Lys Lys Arg Leu Val Glu Lys Gly Leu Glu Ala Cys Cys Ile 865 870 875 880 Glu Gly Val Gln Phe Asp Ile Met Gly Asp Val Glu Ile Ala Arg Cys 885 890 895 Ala Glu Leu Glu Val Gln Lys Arg Glu Leu Tyr Tyr Tyr Leu Ser Ser 900 905 910 Met Pro Phe Pro Gln Gly Val Leu Asp Leu Arg Leu Gly Cys Asn Arg 915 920 925 Asn Asp Thr Lys Cys Glu Thr Cys Gly Arg Ala Leu Met Glu Cys Val 930 935 940 Gly His Trp Gly Tyr Ile Asn Leu Gln Leu Pro Val Phe His Val Gly 945 950 955 960 Phe Phe Lys Tyr Thr Ile Gln Leu Leu Tyr Cys Ile Cys Lys Arg Cys 965 970 975 Ser Ser Leu Leu Leu Pro Phe Asp Thr Val Ala Gln Leu Arg Asp Ala 980 985 990 Arg Leu Arg Arg Ser Asp Asp Pro Leu Ala Arg Ala Val Ile Phe Lys 995 1000 1005 Arg Ile Leu Ser Ser Cys Arg Lys Val Thr Lys Cys Pro Ala Cys 1010 1015 1020 Gly Ala Arg Gln Gly Val Ile Arg Arg Ile Val Lys Pro Thr Met 1025 1030 1035 Asp Gln Phe Met Lys Leu Arg His Val Val Lys Tyr Lys Glu Gly 1040 1045 1050 Gly Lys Ile Val Ile Val Glu Asp Glu Leu Asn Pro Leu Ser Val 1055 1060 1065 Leu Arg Leu Phe Glu Ala Ile Asp Pro Val His Ala Arg Ile Leu 1070 1075 1080 Asn Ile Met Asp Pro Gln Arg Leu Ile Ile Ser Asn Leu Pro Val 1085 1090 1095 Pro Pro Ala Cys Ile Arg Pro Ser Val Ser Leu Gln Gly Gln Gly 1100 1105 1110 Thr Thr Glu Asp Asp Leu Thr Cys Ile Leu Ser Asp Ile Val Glu 1115 1120 1125 Leu Asn Asn Val Met Ala Thr Gln Met Gln Gln Gly Phe Gln Thr 1130 1135 1140 Asn Gln Val Ile Gly Asn Trp Gln Phe Leu Gln Leu Gln Cys Thr 1145 1150 1155 Arg Leu Ile Asn Ala Asp Ala Pro Ala Val Ser Gln Leu Leu Ala 1160 1165 1170 Ala Lys His Ile Ser Lys Pro Gly Arg Gly Ile Cys Gln Arg Leu 1175 1180 1185 Lys Gly Lys Glu Gly Arg Phe Arg Gly Asn Leu Ser Gly Lys Arg 1190 1195 1200 Val Asp Phe Ser Ala Arg Thr Val Ile Ser Pro Asp Pro Asn Ile 1205 1210 1215 Gly Ile Asp Glu Ile Val Ile Pro Glu Tyr Ile Ala Arg Arg Leu 1220 1225 1230 Thr Phe Pro Glu Lys Val Thr Ser Ala Asn Leu Gly Val Leu Gln 1235 1240 1245 Lys Ala Val Leu Asn Gly Val Ser Lys Trp Pro Gly Ala Cys Tyr 1250 1255 1260 Val Met Lys Arg Asp Gly Val Lys Cys Thr Leu Arg Phe Ala Asn 1265 1270 1275 Pro Lys Gln Val Ala Glu Ser Leu Gln Ile Gly Asp Ile Val Glu 1280 1285 1290 Arg His Leu Trp Asn Gly Asp Val Val Leu Phe Asn Arg Gln Pro 1295 1300 1305 Ser Leu His Arg Met Ser Ile Met Ala His Lys Ala Arg Val Met 1310 1315 1320 Pro Gly Ser Thr Phe Arg Phe Asn Glu Cys Val Cys Asn Pro Tyr 1325 1330 1335 Asn Ala Asp Phe Asp Gly Asp Glu Met Asn Leu His Met Pro Gln 1340 1345 1350 Thr Tyr Glu Ala Arg Ala Glu Ala Leu His Leu Met Gly Val Leu 1355 1360 1365 Gln Asn Ile Thr Thr Pro Arg Asn Gly Asp Pro Leu Ile Ala Ala 1370 1375 1380 Thr Gln Asp Phe Leu Ser Ala Ser Tyr Leu Leu Thr Ser Lys Asp 1385 1390 1395 Arg Phe Leu Ser His Gln Glu Phe Cys Gln Leu Leu Cys Tyr Val 1400 1405 1410 Gly Asp Gly Ile Leu His Ala Gln Val Pro Ala Pro Ala Ile Val 1415 1420 1425 Tyr Pro Thr Phe Leu Trp Thr Gly Lys Gln Val Tyr Thr Ala Ile 1430 1435 1440 Leu Arg Gln Ile Gly Ala Val Val Asn Leu Glu Cys Arg Glu Arg 1445 1450 1455 Glu Phe Gln His Pro Glu Pro Asn Leu Phe Gly Arg Met Gln Pro 1460 1465 1470 Asn Phe Met Cys Ile Lys Asp Gly His Val Ile Ile Ser Asn Ser 1475 1480 1485 Glu Leu Leu Cys Gly Ala Leu Ala Lys Lys Thr Leu Gly Ala Ser 1490 1495 1500 Lys Asp Gly Leu Phe Tyr Gln Leu Leu Arg Arg His Gly Pro His 1505 1510 1515 Lys Ala Ala Asp Val Met Leu Lys Val Ser Lys Leu Thr Ser Arg 1520 1525 1530 Trp Val Ser Asp Phe Gly Met Thr Ile Gly Leu Asp Asp Thr Thr 1535 1540 1545 Pro Ser Pro Met Leu Leu Ala Thr Lys Gln Gln Leu Leu Ser Asp 1550 1555 1560 Gly Tyr Ala Lys Val Glu Leu Ala Ile Ala Asn Ala Ala Asn Ile 1565 1570 1575 Glu Pro Phe Pro Gly Cys Thr Arg Lys Glu Thr Leu Glu Leu Gln 1580 1585 1590 Val Lys Gly Ile Leu Asp Asp Leu Arg Asn Gln Ala Gly Lys Ala 1595 1600 1605 Cys Asn Lys Ser Leu Ser Ala Asn Asn Lys Pro Met Ile Met Phe 1610 1615 1620 Asn Ser Gly Ala Lys Gly Ala Leu Ile Asn Ile Ala Gln Met Ile 1625 1630 1635 Ala Cys Val Gly Gln Gln Asn Val Met Gly Gln Arg Ile His His 1640 1645 1650 Gly Phe Ile Gly Arg Thr Leu Pro His Phe Glu Val Gly Cys Ile 1655 1660 1665 Asp Ala Lys Ser Arg Gly Phe Val Ser Asn Ser Phe Phe Ser Gly 1670 1675 1680 Leu Asp Pro Ala Glu Phe Trp Phe His Thr Met Ser Gly Arg Glu 1685 1690 1695 Gly Leu Ile Asp Thr Ala Val Lys Thr Ser Glu Thr Gly Tyr Met 1700 1705 1710 Gln Arg Arg Leu Met Lys Ala Leu Glu Asp Leu Ala Ile Cys Tyr 1715 1720 1725 Asp Tyr Thr Val Arg Thr Ser Asp Gly Gln Ile Val Gln Phe Ile 1730 1735 1740 Tyr Gly Asp Asp Gly Leu Gly Ala Ser Gly Ala His Ala Thr Thr 1745 1750 1755 Pro Lys Ala Leu Gln Glu Thr Leu Ala His Val Leu Thr Leu Ser 1760 1765 1770 Arg Phe Gln Arg Thr Pro Thr Ile Leu Asn Ser Arg Ala Pro Gly 1775 1780 1785 Pro Asn Ser Lys Gly Asp Leu Arg Leu Pro Leu Pro Ser Gly Asp 1790 1795 1800 Gly Asp Asp Glu Asn Phe Glu Cys Gly Ile Val Pro Lys Cys Lys 1805 1810 1815 Leu Ala Met Pro Pro Lys Val Lys Ala Lys Ala Ser Ala Arg Ala 1820 1825 1830 Ser Trp Arg Thr Ser Gln Val Gly Thr Pro Leu Asp Glu Ala Thr 1835 1840 1845 Ser Ala Gln Ile Asn Arg Asn Met Tyr Ala His Trp Val Val His 1850 1855 1860 Val His Leu Asp Pro Glu His Ala Lys Ala Pro Leu Phe Gly Asp 1865 1870 1875 Glu Val Leu Asp Trp Val Ala Leu Leu Glu Pro Leu Cys Arg Glu 1880 1885 1890 Pro Leu Pro Arg Cys Met Gln Glu Ser Val Thr Ser Met Asp His 1895 1900 1905 Thr Ser Glu Pro Arg Ile His Ala Ser Ser Met Glu Ile Asp Lys 1910 1915 1920 Arg Val Asn Gly Cys Ser Met Lys Ala Thr Asn Thr Gly Pro Arg 1925 1930 1935 Phe Ser Ala Val Leu Leu Asp Thr Ile Arg Gln Trp Ala Ala Arg 1940 1945 1950 Leu Gln Thr Leu Asp Pro Glu Ile Gln Arg Glu Tyr Glu Ser Ser 1955 1960 1965 Gly Met Asp Leu Val Gln Phe Arg Ala Phe Lys Ile Pro Pro Gln 1970 1975 1980 Asp Arg Ile Ser Val Leu Gln Ile Tyr Glu Phe Leu Arg Cys Ala 1985 1990 1995 Trp Ser Asp Tyr Leu His Gly Ile Cys Glu Pro Gly Glu Ala Ile 2000 2005 2010 Gly Ala Leu Gly Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln Met 2015 2020 2025 Thr Leu Lys Thr Phe His Phe Ala Gly Val Ala Ser Met Asn Val 2030 2035 2040 Thr Leu Gly Val Pro Arg Ile Lys Glu Ile Ile Asn Ala Ala Ser 2045 2050 2055 Val Ile Gln Thr Pro Ile Ile Glu Val Pro Leu Ala Lys Lys Asp 2060 2065 2070 Ser Tyr Asp Phe Ala Lys Ser Val Arg Ala Lys Ile Glu Arg His 2075 2080 2085 Thr Leu Glu Gln Val Val His Ser Ile Lys Gln Val Tyr Thr Pro 2090 2095 2100 Gly Ala Thr Leu Leu Leu Val Ser Leu Asp Ser Gln Tyr Ile Gln 2105 2110 2115 Gln Asn Met Leu Gln Leu Asp Ala Ser Ser Val Cys Ala Val Ile 2120 2125 2130 Arg Asn Ser Asn Leu Ile Thr Lys Phe Lys Leu Ser Lys His Asn 2135 2140 2145 Ile Glu Ala Pro Gln Lys Trp Leu Val Ser Ile Arg Leu Val Ala 2150 2155 2160 Ser Glu Ala Leu Leu Phe Gln Leu Asn Ala Leu Val Ala Ala Leu 2165 2170 2175 Gly Gln Leu Val Val Cys Gly Val Lys Asp Ile Lys Arg Cys Val 2180 2185 2190 Val Lys Arg Glu Gln Lys Asp Val Ile Asn Ser Leu Thr Pro Gly 2195 2200 2205 Ala Thr Phe Glu Tyr Ala Leu Ala Val Glu Gly Tyr Gly Leu Gln 2210 2215 2220 Gln Val Leu Gly Ile Phe Gly Val Asp Ala His Arg Val Ile Ser 2225 2230 2235 Asn His Val Ala Glu Val Ala Lys Val Leu Gly Ile Glu Ala Ala 2240 2245 2250 Arg Leu Val Ile Val Thr Glu Ile Lys Lys Ser Met Asp Ala Tyr 2255 2260 2265 Gly Ile Asp Ile Asp Gly Arg Tyr Met Lys Leu Leu Gly Asp Val 2270 2275 2280 Met Thr Phe Arg Gly Glu Val Val Gly Ile Asn Arg Phe Gly Ile 2285 2290 2295 Gln Lys Met Arg Ala Ser Ser Leu Met Leu Ala Ser Phe Glu Glu 2300 2305 2310 Thr Asn Glu His Leu Phe Gln Ala Ala Val His Gly Arg Arg Asp 2315 2320 2325 Pro Ile Lys Gly Val Ser Glu Cys Ile Ile Met Gly Lys His Ile 2330 2335 2340 Ala Leu Gly Thr Gly Ala Phe Asp Leu Leu Tyr Arg Glu 2345 2350 2355 <210> 34 <211> 681 <212> PRT <213> babesia duncani <400> 34 Met Ala Asn Gly Gly Leu Tyr Val Phe Pro Leu Leu Leu Cys Met His 1 5 10 15 Ser Val Tyr Ala Leu Gln Cys Pro His Ala His Arg Ala Cys Phe Leu 20 25 30 Lys Tyr Asn Gly Ile Tyr Thr Ser Lys Ala Asn Lys Leu Gly Val Leu 35 40 45 Asp Val Val Asn Val Glu Asp Asn Ala Leu Asp Leu Glu Asp Val Val 50 55 60 Pro Leu Gln Glu Val Tyr Lys Phe Phe Asn Asn Tyr Leu Met Pro Phe 65 70 75 80 Tyr His Lys Arg Val Ser Gln Asn Tyr Gly Thr Asn Val Pro Ile Ile 85 90 95 Ile Ser Cys Ser Gly Gly Val Asp Ser Met Ala Leu Leu His Thr Phe 100 105 110 Gly Leu Ile Lys Glu Asn Ser His Thr Phe Ile Lys Lys His Pro Ile 115 120 125 Asn Tyr Ile Asp Gly Ser Asn Ala Val Ile Ala Glu Thr Ala Ser Asn 130 135 140 Val Leu Lys Tyr Ile Phe Glu Asn Val Asn Val Ile Tyr Phe Asp His 145 150 155 160 Lys Val Arg Ser Asp Thr Lys Val Asp Ile Glu Ile Ile Glu Asn Ala 165 170 175 Cys Lys Lys Tyr Asn Phe Asn Phe Asn Val Gln Glu Leu Asp Cys Asn 180 185 190 Asp Ser Tyr Phe Ser Asn Leu Glu Gly Gly Phe Gln Ala Asn Ser Arg 195 200 205 Lys Trp Arg Arg Arg Glu Leu Lys Lys Tyr Val Met Glu Leu His Ser 210 215 220 Ser Lys Met Leu Ser Asn Glu Gly Lys Asn Lys Ile Gly Ile Arg Asn 225 230 235 240 Gly Ser Tyr Asn Ser Ile Thr Thr Asn Lys Gln Asp Gly Leu Asn Ser 245 250 255 Asn Ser Ile Gly Ile Val Phe Met Gly His His Ala Asn Asp Asn Ile 260 265 270 Glu Thr Phe Phe Met Lys Phe Ile Arg Gly Thr His Leu Leu Gln Met 275 280 285 Serving Glu with Asn Asp Gln Serving Phe Leu Asp Serving Lys Asp with Arg Pro 290,295,300 Leu Ile Arg Pro Phe Ile His Leu Pro Lys Asn Ala Leu His Gln Phe 305 310 315 320 Met Gln Asp Phe Arg Phe Gln Tyr Asn Glu Asp Ser Thr Asn Val Leu 325 330 335 Phe Asp Tyr Gly Arg Asn Gln Phe Arg Lys Leu Val Met Pro Asn Leu 340 345 350 Glu Tyr Isolation Met Ser Isolation of Asn Lys Cys Gln Asn Asp Lys Ala Isolation 355 360 365 Asp Leu Leu Asp Lys Arg Ile His Val Leu Ser Lys Gln Ala Ser Asn 370 375 380 Phe Arg Asn Asp Ile Glu Phe Gln Ile Gln Met Phe Lys Val Tyr Leu 385 390 395 400 Lys Ser Lys Tyr Gly Asp Leu Leu Pro Ile Lys Lys Arg Tyr Met 405 410 415 Asn Arg Met Gly Glu Ile Ser Asp Phe Tyr Lys Arg Leu Tyr Phe 420 425 430 Asn Arg Tyr Thr Asn Only Has His Asn With Gln Glu Leu Lys Tyr 435 440 445 Phe His Asp Leu Asn Ile Pro Ile Met Asp Leu Phe Phe Val Asp Glu 450 455 460 Trp Your Ile Your Glu Ser Lys Your Your Arg Glu Glu Val Your Tyr Asp 465 470 475 480 Phe Phe Ser His His Phe Arg Lys Pro Leu Phe Tyr Asn Ala Phe Thr 485,490,495 Lys Ile Val Asp Arg Leu Glu Val Asn Phe Ser Glu Gly Ser Ile Lys 500 505 510 Gln Tyr Cys Leu Ser Lys Asp Val Ser Met Ser His Gln Gly Ser Leu 515,520,525 Leu Lys Val Lys His Arg Pro Glu Lys Asn Glu Lys Val Leu Ile Phe 530 535 540 Lys Asp Asp Leu Cys Ser Phe Ser Val Leu Asp Asn Leu Gln Leu Phe 545 550 555 560 Val Glu Lys Ala Glu Gly Tyr Thr Arg Asn Val Phe His Leu Leu Phe 565 570 575 Lys Val Pro Met Tyr Ala Thr Thr Glu Ser Ile Asp Phe Asp Ile Arg 580 585 590 Leu Phe Arg Asn Asp Asp Val Leu Pro Ser Lys Ile Leu Trp Asn Arg 595 600 605 Glu Ala Gly Ser Leu Leu Thr His Met Lys Ile Lys His Ile Ile Lys 610 615 620 Asp Tyr Ile Pro Val Ile Ala Met Ala Gly Thr Asn Lys Ile Val Gly 625 630 635 640 Phe Tyr Gly Phe Asn Ile Ile Pro Pro Tyr His Cys Arg Gly Arg Gln 645 650 655 Glu Val Thr Tyr Ser Phe Val Asp Val Ala His Gly Ser Thr Glu Tyr 660 665 670 Arg Glu Tyr Ser Ile Arg Val Thr Arg 675 680 <210> 35 <211> 1523 <212> PRT <213> babesia duncani <400> 35 Met Gly Phe Phe Ile Gln Ser Gln Leu Leu Ser Thr Leu Trp Ile Leu 1 5 10 15 Ile Val Ile Pro Gln Asn Val Gln Cys Leu Arg Asn Asn Ser Arg Asn 20 25 30 Asn Ser Leu Ala Phe Ala Ser Gly Tyr Ala His Ser Asn Val Arg Asn 35 40 45 Ser Leu Asp Ser Leu Asn Gly Leu Pro Asn Leu Ile Asn Arg Lys Glu 50 55 60 Pro Thr Cys Gln Asp Gly Phe Lys Leu Phe Gly Val Pro Arg Met Tyr 65 70 75 80 Gly Trp Met Ile Glu Asn Leu Gly Lys Ile Asn Gln Ser Phe Asp Thr 85 90 95 Cys Asp Phe Tyr Glu Asp Val Asp Tyr Phe Tyr Ile Asp Met Asn Ala 100 105 110 Val Ile His Ser Ala Thr His Gly Asn Met Ser Pro Ile Val Glu Ile 115 120 125 Glu Asp Glu Gln Arg Met Arg Arg Ile Thr Ser Thr Leu Leu Lys Leu 130 135 140 Phe His Met Ile Lys Pro Lys Lys Val Met Tyr Leu Ala Val Asp Gly 145 150 155 160 Val Cys Pro Ser Ala Lys Ile Asn Gln Gln Arg Thr Arg Arg Phe Arg 165 170 175 Leu Ala Lys Lys Val Glu Asp Leu Thr Ala Arg Val Gln Asp Ile Cys 180 185 190 Glu Met Lys Pro Ile Glu Asp Tyr Asn Ile Asp Lys Leu Pro Cys Gly 195 200 205 Ser Tyr Asp Asn Val Thr Phe Asn Pro Asn Tyr Ile Ser Pro Gly Thr 210 215 220 Glu Phe Met Gln Met Phe Asp Ser Glu Ile Lys Asn Trp Leu Ala Ile 225 230 235 240 Lys Thr Leu Glu Lys Gln Trp Gly Asp Cys Leu Val Ile Tyr Asp Gly 245 250 255 Ala Asn Ile Pro Gly Glu Gly Glu Gln Lys Ile Tyr Glu Phe Met Arg 260 265 270 Lys Leu Asn Glu Ser Lys Val Lys Ser Arg Asn Lys Asn His Leu Val 275 280 285 Tyr Gly Leu Asp Ala Asp Ile Met Met Leu Ser Leu Leu Thr Lys Met 290 295 300 Pro Asn Val Cys Val Leu Arg Glu Lys Arg Asp Tyr Thr Pro His Ile 305 310 315 320 Leu Ser Lys Ile Lys Pro Glu Pro Tyr Phe Thr Pro Glu Thr Gly Ile 325 330 335 Val His Tyr His Ala Asn Asp Tyr Ile Asp Leu Glu Ala Lys His Phe 340 345 350 Asp Will Will Be Met Met Asp With Arg Arg Ala Leu Tyr Asn Arg Cys 355 360 365 Tyr Val Gly Leu Lys Tyr Asp Leu Ala Asn Ile Pro Phe Leu 370 375 380 Asn Gln Glu Asn Val Pro Asn Arg Leu Ala Asp Asp Phe Val Leu Leu 385 390 395 400 Ser Phe Leu Ala Gly Asn Asp Phe Leu Pro His Leu Pro Thr Val Asp 405 410 415 Leu Glu Phe His Thr Phe Ser Asp Met Leu Asn Ser Tyr Phe Phe Met 420 425 430 Leu Pro Arg Leu His Gly Phe Ile Thr Arg Gly Tyr Arg Ile His Met 435 440 445 Gly Arg Leu Gln Lys Leu Phe Arg Val Leu Gln Arg Gln Glu Val His 450 455 460 Val Phe Lys Glu Lys Ala Gln His Glu Ser Val Pro Glu Tyr Arg Asp 465 470 475 480 Val Thr Lys Tyr Ala Glu His Tyr Tyr Arg Val Lys Lys Asn Ile Asn 485 490 495 Tyr Lys Asn Arg Asn Gln Val Thr Arg Met Cys Gln Glu Tyr Ile Lys 500 505 510 Gly Leu Val Trp Asn Leu Tyr Tyr Tyr Tyr Lys Gly Cys Pro Ser Trp 515 520 525 Asn Trp Cys Tyr Lys Tyr His Tyr Ala Pro Leu Val Ser Asp Leu Ser 530 535 540 Gln Thr Ser Gly Val Phe Val Ser Phe Lys Arg Gly Arg Pro Ile Lys 545 550 555 560 Pro Leu Glu His Leu Leu Ala Val Ser Pro Pro Asn Gly Asn Glu Leu 565 570 575 Leu Pro Glu Gln Tyr Arg Lys Leu Ser Ala Ser Pro Asn Gly Glu Leu 580 585 590 Ala Glu Phe Phe Pro Thr Asp Tyr Glu Ile Cys Glu Asp Gly Lys Val 595 600 605 Asn Glu Trp Glu His Val Val Lys Leu Pro Phe Leu Asn Thr Asn Lys 610 615 620 Leu Val Thr His Ala Glu Gln Ala Asn Gln His Leu Lys Tyr Asn Ser 625 630 635 640 Leu Ser Lys Asn Lys Leu Gly Arg Val Asn Val Tyr Lys Cys Arg Pro 645 650 655 His Asn Val Asn Lys Ser Gly Asp Asn Arg Leu Ile Phe Asp Asp Leu 660 665 670 Thr Lys Lys Gly Leu Ile Val Arg Asp Gly Met His Tyr Gly Ala Thr 675 680 685 Phe Ser Val Tyr Glu Glu Arg Pro Gly Leu Ala His Ser Ser Cys Leu 690 695 700 Ile Phe Ala Arg His Gly Gln Thr Pro Ile Met Ile Lys Asp Leu Val 705 710 715 720 Arg Trp Thr Arg Ile Ser Gln Ala Ala Asn Lys Arg Val Leu Ile Ile 725 730 735 Thr Ile Leu Tyr Lys Thr Met Asn Thr Ser Gly Trp Ser Ser Asp Phe 740 745 750 Ser Ser Leu Ser Asn Ser Asp Lys Ile Thr Gly Lys Asp Arg Ile Asn 755 760 765 Glu Gln Glu Ser Ile Ser Val Pro Ser Gly Leu His Cys Gly Pro Ala 770 775 780 Gly Arg Arg Thr Leu Ile Lys Trp Ile Glu Glu Asn Tyr Arg Val Arg 785 790 795 800 Lys Gly Met Asp Asp Thr Asn Pro Gly Val Val Ala Cys Arg Leu Trp 805 810 815 Gln Asp Ser Gln Gly Phe Ser Asp Pro Val Ser Lys Ala Ala Ile Asp 820 825 830 Leu Leu Arg Leu Gln Gly Ile Pro Ala Asn Val Thr Tyr Lys Thr Leu 835 840 845 Phe Glu Gln His Leu Ser Lys Met Leu Ser Ser Leu Ile Asn Gln Ser 850 855 860 Arg Asn Ser Gln Ala Arg Leu Tyr Ser Ile Ala Glu Lys Met Ile Gly 865 870 875 880 Met Phe Gln Val Ala Glu Ile Gln Pro Leu Ile Cys Asp Val Leu Asp 885 890 895 Gln Leu Asp Glu Ile Pro Gln Phe Ala Leu Pro Lys Leu Leu Asp Asp 900 905 910 Ala Ala Ser Ala Asn Asn Phe Tyr Lys Ile Cys Asn Asp Gly Leu Lys 915 920 925 Arg Lys Ile Trp Ala Thr Ser Ala Val Arg Leu Tyr Glu Glu Met Leu 930 935 940 Pro Leu Phe Gln Glu Ala Val Leu Cys Ile Gln Leu Gly Val Leu Glu 945 950 955 960 Pro Arg Met His His Ala Ser Phe Ile Gln Ser Cys Arg Glu Arg Tyr 965 970 975 Glu Ile Val Ile Glu Gln Ile Cys Gln Met Ile Gly Asp Cys Lys Ser 980 985 990 Gln Ala Ser Arg Gln Val Phe Arg Leu Thr Met Arg Ile Ile Lys Val 995 1000 1005 Leu Tyr Val Lys Ser Ile Leu Gly Asp Lys Gly Asp Phe Gln Ile 1010 1015 1020 Tyr Phe Thr Pro His Asp His Leu Asp Thr Ala Leu Lys Leu Asn 1025 1030 1035 Trp Arg Asp Leu Ala Ala Arg Ser Val Gly Ile Cys Phe Lys Ser 1040 1045 1050 Leu Gln Leu Glu Glu Leu Asp Glu Ala His Asp Ser Phe Ser Ser 1055 1060 1065 Thr Asp His Ser Ser Phe Cys Ala Leu Ala His Ser Ile Ile Ser 1070 1075 1080 Arg His Gln Asp Met His Lys Ile Thr Ser Ser Asp Met Gln Asp 1085 1090 1095 Leu Glu Ser Phe Tyr Thr Leu Trp Ser Leu Val Asp Thr Val Ile 1100 1105 1110 Ala Ser Pro Cys Met Ser Leu Asp Asn Glu Gln Ile Ala Ser Val 1115 1120 1125 Leu Asn Val Val Leu Gly Asp Leu Arg Ile Arg Asp Glu Ile Asp 1130 1135 1140 Leu Phe Asp Ala Ser Phe Val Leu Gly His Phe Glu Phe Leu Ile 1145 1150 1155 Lys Ile Ser Lys Tyr Ile Val Thr Arg Ser Ile Asn Ile Asn Glu 1160 1165 1170 Gln Leu Pro Glu Asp Gln Asp Thr Leu Gly Gln Trp Phe Ser Leu 1175 1180 1185 Ala Ser Leu Gly Leu Ser Cys Gly Tyr Ile Gly Ala Cys Gln Phe 1190 1195 1200 Leu Phe Arg Ala Gln Trp Asn Asn Asp Thr Cys Ile Trp His Phe 1205 1210 1215 Pro Thr Glu Thr Glu Pro Gly Lys Pro Ile Ser Leu Ser Lys Leu 1220 1225 1230 Leu Gly Tyr Thr Phe Pro Tyr Asn Arg Ser Asp Gln Met Cys Leu 1235 1240 1245 Asp Thr Leu Pro Pro Phe Phe Tyr Lys Ile Val His Gly Gln Ala 1250 1255 1260 Ser Pro His Leu Ser Glu Thr Ser Pro Val Arg Asn Pro Tyr Glu 1265 1270 1275 Ala Asn Lys Ala Ser Leu Arg Asn Leu Leu Cys Leu Tyr Leu Pro 1280 1285 1290 Met Val Asp Val Trp Lys Phe Lys Arg Ala Met Met Asp Leu Lys 1295 1300 1305 Ala Phe Glu Gln Asn Gly Tyr Gly Thr Leu Leu Asn Ser Phe Lys 1310 1315 1320 Arg Gln Thr Phe Gln Thr Glu Lys Leu Leu Phe Tyr Met Gln Asp 1325 1330 1335 Met Ala Ile Arg Asp Phe Glu Ser Asp Asp Tyr Asp Trp Thr Ile 1340 1345 1350 Ala Arg Lys Leu Tyr Gln Asn Leu Glu Arg Leu Gln Ala Leu Lys 1355 1360 1365 Leu Ala Thr Pro Pro His Gly Thr Val Met Asp Pro Lys Ser Pro 1370 1375 1380 Gln Pro His Val Asp Asp Gly Lys Arg Leu Met Gly Thr Ile Leu 1385 1390 1395 Ile Gln Gly Asp Ile Thr Cys Gly Phe Ile Arg Met Met Gly Val 1400 1405 1410 Ser Met Val Glu Ala Ser Asp Glu Met Ala Arg Arg Leu Glu Asn 1415 1420 1425 Tyr Trp Lys Asn Leu Leu Gln Pro Tyr Met Cys Cys Met Gln Phe 1430 1435 1440 Arg Leu Leu Arg Met Leu Phe Ser Asn Trp Thr Lys Ile Ser Ser 1445 1450 1455 Phe Ser Leu Asp Val Leu Cys Lys Met Val Lys Gly Tyr Pro Ile 1460 1465 1470 Val Ala Phe Leu Pro Leu Phe Thr Lys Ala Pro Asn Cys Asp Ile 1475 1480 1485 Ser Thr Ala Leu Gly Arg Leu Ser Ala Ser Leu Gln Gly Thr Leu 1490 1495 1500 Pro Asn His Ser Ser Lys Gly Trp His Arg Ile Val Phe Thr Met 1505 1510 1515 Tyr Asn Lys His Ser 1520 <210> 36 <211> 825 <212> PRT <213> babesia duncani <400> 36 Met Lys Leu Gln Ile Asn Ser Phe Asn His Ile Phe Phe Ile Lys Gln 1 5 10 15 Asn Ile Arg Thr Asn Leu Phe Lys Leu Ser Gln Lys Pro His Pro Phe 20 25 30 Asn Leu Lys Phe Phe Arg Gln Tyr Ser His His Glu Ile Phe Thr Ser 35 40 45 Ile Lys Leu Ala Ser Asn Lys Ser Glu Met Ala Ser Val Thr Gln Ile 50 55 60 Leu Leu Asn Arg Ser Asn Tyr Lys Gly Val Val Thr Leu Asp Asn Ser 65 70 75 80 Thr Val Val Ser Ala Asn Asp Ile Val Leu Tyr Ser Glu Phe Asn Ser 85 90 95 Lys Ile Ser Phe Ser Leu Thr Leu Asp Thr Leu Lys Lys Leu Thr Lys 100 105 110 Leo Gln Thr Pro Cys Lys Val Val Trp Asn Tyr Val Ile Asp Ser Ile 115 120 125 Leu Ser Asp Ser Ser His Phe Thr Pro Asn Glu Ile Ala Lys Ile Leu 130 135 140 Val Tyr Ile Leu Asn Ile Lys Phe Asn Asp Ile Phe Ile Lys Ser Lys 145 150 155 160 Ile Glu Leu Ala Ser Glu Thr Leu Ile Glu Lys Leu Asn Gly Ser Leu 165 170 175 Ser Leu Met Val Gly Phe Ser Val Ile Asp Ile Lys Arg Ala Gly Leu 180 185 190 Arg Asn With Ser Asp Thr With Arg His Asp Ala Glu Phe Asp Lys Leu 195 200 205 Asp Ser Met Asp Phe Glu Ile Ile Trp Lys Leu Trp Tyr Thr Leu Ser 210 215 220 Lys Gln Arg Gly Asn Glu Arg And Arg Gly Leu Phe Glu Tyr Leu 225 230 235 240 Glu Arg Gly Lys Asp Lys Val Tyr Lys Phe Asp Leu Pro Lys Val Ile 245 250 255 Arg Ser Met Asp Ile Ile Leu Ser Asn Ser Lys Ser Leu Asp Leu Leu 260 265 270 Glu Lys and Glu Lys and Lys Arg and Asn and Tyr 275 280 285 Asn Ser Asp Asn Ile Pro Thr Phe Gly Gly Ser Ser Asn Ile Tyr Met 290,295,300 Thr Thr with Gln and Lys with Lys with Tyr and Gly with Asn and Cys 305 310 315 320 Lys Arg Asn Pro Lys Ile Phe Glu Asn Ile Val Lys Glu Cys Ala 325 330 335 Met Leu Ser Leu Val Asn Phe Leu Lys Gln Val Lys Glu Ile Thr Ser 340 345 350 Arg Ser Leu Glu Val His Cys Arg Leu Tyr Asn His Leu Lys Asn Ile 355 360 365 Asn Val Glu Asn Thr Asn Met Lys His Asn Val Arg Ile Glu Ala Ile 370 375 380 Lys Arg Ser Ser Asn Val His Ala Lys Met Phe Val Tyr Cys Val Glu 385 390 395 400 Phe Leu Asn Asn Phe Asp Leu Ile Thr Lys Ala Asn Tyr Asn Asn Ala 405 410 415 Ser Ser Tyr Ser Lys Ala Thr Ser Asp Asn Lys Arg Ser Thr Asp Leu 420 425 430 Asp His Thr Ile Phe Asp Ile Cys Thr Asn Leu Leu Arg Cys Thr Ala 435 440 445 Gln Ser Ser Phe Leu Ile His Asn Val Thr Met Tyr Cys Arg Ser Ile 450 455 460 Tyr Gln Leu Leu Val Leu Ala Leu Tyr Asn Thr Cys Thr Gly Ile Asn 465 470 475 480 Glu Ser Phe Val Lys Ala Ala Leu Ser Ser Ile Ser Asn Ile Gln Ala 485 490 495 Thr Thr Leu Gln Met Asp Arg Asp Asn Trp Asp Ile Ser Ser Val Ile 500 505 510 Arg Asn Leu Ser Tyr Ile Asp Lys Gly Ile Ser Val Leu Ala Asp Ile 515 520 525 Ser Tyr Ser Ser Ile Ile Leu Glu Pro Ile Gln Asn Ala Asn Ala Glu 530 535 540 Ile Val Ser Lys Cys Ser Ser Lys Tyr Glu Glu Val Leu Met Gly Gly 545 550 555 560 Glu Ile Leu Gln Leu Asp Lys Leu Val Tyr Cys Thr Leu Leu Asn Lys 565 570 575 Tyr Asn Ile Ile Asp Gly Thr Met Leu Asp Val Leu Leu Gln Phe Ile 580 585 590 Lys Ala Asn Glu Leu Thr Ser Arg Glu Leu Cys Met Phe Cys Asp Leu 595 600 605 Leu Leu Lys Thr Arg Glu Met Leu Met Asp Asp Cys Asp Lys Arg Asn 610 615 620 Asn Val Leu Ala Lys Leu Leu Pro Leu Ala Leu Glu Leu Leu Lys Ser 625 630 635 640 Ile Asp Phe Asp Phe Asn Lys Arg Thr Leu Lys Asp Leu Leu Leu Ile 645,650,655 Leu Glu Cys Leu Gly Ala Phe Gly Phe Ser Cys Ala Asp Asp Leu Ser 660,665,670 Lys Arg with Glu His Gly Ala Lys Thr with Gln Ser 675,680,685 Lys Leu Tyr Ser Ile Val Asn Asp Asp Tyr Lys Arg Ile Arg Leu 690,695,700 Pro Gly With Leu Lys Gln Arg Gly With Asn And Thr Ala 705 710 715 720 Lys Lion Val Asn Val Lion Asp Is Asp Tyr Asn Lion Glu 725 730 735 Thr Glu His Asn To Gly Asp Asp To Tyr To Val Asp Lys Ala 740,745,750 Tyr Phe Ala Arg Lys Arg Leu Leu His Gln Arg Asn Ser Ser Asn Pro 755,760,765 Arg Lys Lys Thr Lys Val Asp Tyr Asn Asn Ser Gly Ser His His Met 770,775,780 Phe Ile Ile Asp Ser Ser Val Ala Lys Ala Phe Ile Lys Cys Asn Lys 785,790,795,800 Gly Thr His Ser Ser Ser Lys Leu Tyr Lys Ile Leu Val Ser Lys Tyr 805 810 815 Gln Ser Ser Ser Ser Ser Met Ala Leu 820 825 <210> 37 <211> 374 <212> PRT <213> babesia duncani <400> 37 Met Gln Gly Gly Trp Leu Leu Val Cys Ile Val Gly Phe Leu Ala Cys 1 5 10 15 Phe Gly Ala Ser Thr Lys Pro Asn Asp Lys Lys Ala Thr Asn Glu Glu 20 25 30 Leu Thr Cys Pro Ala Val Asn Asp Leu Gln Gly Thr Pro Ile Asp Leu 35 40 45 Gln Tyr Thr Phe Asp Arg Leu Asp Met Thr Ser Leu Ser Arg Leu Leu 50 55 60 Ala Ile Gln Asn Met Tyr Ser Lys Arg Asn Pro Arg Asn Ile Arg Ile 65 70 75 80 Pro Lys Phe Trp Asn Thr Asp Val Ala His Gly Ile Trp Ser Arg Phe 85 90 95 Arg Ile Tyr Gly Thr Asn Leu Val Tyr Lys Thr Ser Arg Gly Asp Gly 100 105 110 Ser Cys Leu Phe Trp Ser Val Ser Asp Ser Leu Arg Leu Gly Gly Phe 115 120 125 Thr Ile Lys Lys Ile Lys Glu Asn Leu Asp His Tyr Gly Thr Lys Asn 130 135 140 Arg Gly Ile Tyr Glu Ala Ile Met Ser Leu Pro Asn Asp Asp Glu Tyr 145 150 155 160 Leu Thr Met Gln Asp Ile Gln Arg Ile Ala Thr Ile Gly Phe Val Gly 165 170 175 Phe Asp Pro Asp Val Glu Ala Ser Val Lys Gln Trp Asp Arg Glu Pro 180 185 190 Ile Leu Ser His Leu Glu Thr Val Lys Ser Leu Lys Thr Ala Tyr Met 195 200 205 Gly Asp Val Ile Pro Phe Asp Leu Gly Cys His Arg Phe Thr Ser Phe 210 215 220 Arg Ala Val Asp Asp Phe Tyr Asn Gly Ile Ala Asn Asp Ala Thr Cys 225 230 235 240 Ile Lys Ala Gly Arg Asp Leu Phe Asn His Thr Ile Lys Tyr Leu Ala 245 250 255 Ser Gly Ala Trp Gly Tyr Glu Ile Asp Ile Tyr Ala Ile Glu Thr Ala 260 265 270 Lew Asn Lew Lys Ile Val Lew Ile Ser Tyr Asn Thr Gly Ser Leu Val 275 280 285 Cys Tyr Tyr Trp Ser Glu Asp Tyr Val Pro Gln Ser Met Ile Leu 290,295,300 Tyr Tyr His Asp Ser Arg His Phe Asp Val Ala Gly Leu Val Asp Met 305 310 315 320 Phe Lys Val Pro Asn Val Arg Asn Pro Arg Ala Lys Val Leu Thr Ser 325 330 335 Phe His Ile Arg Glu Met Pro Met Ala Leu Ala Ile Ile Leu Lys Asp 340 345 350 Asp Cys Arg With Thr Lys Arg Asn Glu Arg Phe Ser Phe Gly Asn Glu 355 360 365 Asp Has Thr His Has Tyr 370 <210> 38 <211> 654 <212> PRT <213> babesia dunkin <400> 38 Met Gln Met Phe Asn Arg Phe Leu Lys Ala Ser Val Ala Leu Leu Ala 1 5 10 15 Val Ala Ser Phe Gly Ile Gln Tyr Ile Phe Ala Lys Gly Ser Asn Ser 20 25 30 Gly Lys Ile Glu Gly Pro Ile Ile Gly Ile Asp Leu Gly Thr Thr Tyr 35 40 45 Ser Cys Val Gly Ile Tyr Lys Asn Gly Arg Val Glu Ile Ile Ala Asn 50 55 60 Glu Met Gly Asn Arg Ile Thr Pro Ser Tyr Val Ser Phe Val Glu Gly 65 70 75 80 Thr Gln Lys Val Gly Glu Ala Ala Lys Ser Glu Ala Thr Ile Asn Thr 85 90 95 Glu Ser Thr Val Phe Asp Val Lys Arg Leu Ile Gly Arg Lys Phe Thr 100 105 110 Asp Arg Asp Val Gln Glu Asp Met Lys Leu Leu Pro Tyr Lys Ile Ile 115 120 125 Asn Lys Ser Thr Arg Pro Tyr Ile Ser Leu His Asp Gly Lys Glu Gln 130 135 140 Arg Thr Phe Ala Pro Glu Glu Ile Ser Ala Met Val Leu Lys Lys Met 145 150 155 160 Lys Gln Val Ala Glu Ser Tyr Leu Gly Lys Glu Val Lys Lys Ala Ile 165 170 175 Ile Thr Val Pro Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ser Thr Lys 180 185 190 Asp Ala Gly Ala Ile Ala Gly Leu Asp Val Val Arg Ile Ile Asn Glu 195 200 205 Pro Thr Ala Ala Ala Ile Ala Tyr Gly Leu Asp Lys Ala Asn Ala Glu 210 215 220 Ser Asn Ile Leu Val Tyr Asp Leu Gly Gly Gly Thr Phe Asp Val Ser 225 230 235 240 Val Leu Thr Leu Asp Ser Gly Val Phe Glu Val Ile Ala Thr Gly Gly 245 250 255 Asp Thr His Leu Gly Gly Glu Asp Phe Asp Arg Arg Val Met Asp His 260 265 270 Phe Ile Asp Ile Phe Lys Lys Lys His Lys Val Asn Ile Arg Asp Asn 275 280 285 Lys Gln Ser Leu Gln Lys Leu Arg Lys Glu Val Glu Ala Ala Lys Arg 290 295 300 Thr Leu Ser Ser Thr Thr Glu Val Leu Val Glu Val Glu Asn Leu Ile 305 310 315 320 Asn Gly Ile Asp Phe Ser Glu Lys Leu Thr Arg Ala Lys Phe Glu Ser 325 330 335 Leu Asn Ala Glu Leu Phe Glu Lys Thr Leu Ala Thr Val Lys Lys Val 340 345 350 Val Glu Asp Ala Asp Ile Pro Ile Arg Asp Ile Asn Gln Val Val Leu 355 360 365 Val Gly Gly Ser Thr Arg Ile Pro Arg Ile Arg Glu Met Ile Lys Glu 370 375 380 Tyr Phe Gly Lys Glu Pro Asp Tyr Gly Ile Asn Pro Asp Glu Ala Val 385 390 395 400 Ala Phe Gly Ala Ala Met Gln Gly Gly Ile Leu Ser Gly Glu Ser Ser 405 410 415 Asp Asn Leu Leu Leu Leu Asp Val Cys Pro Leu Ser Leu Gly Ile Glu 420 425 430 Thr Leu Gly Glu Val Met Ser Val Ile Ile Pro Arg Asn Thr Met Ile 435 440 445 Pro Ala His Lys Ser Gln Val Phe Ser Thr Ser Val Asp Asn Gln Pro 450 455 460 Met Val Thr Ile Lys Val Tyr Gln Gly Glu Arg Lys Leu Thr Lys Asp 465 470 475 480 Asn Val Ile Leu Gly Lys Phe Asp Leu Ser Gly Ile Pro Pro Ala Pro 485 490 495 Arg Gly Val Pro Gln Ile Glu Val Thr Phe Asp Ile Asp Thr Asn Gly 500 505 510 Ile Leu Ser Val Ser Ala Glu Glu Lys Gly Ser Gly Asn Lys His Asn 515 520 525 Ile Val Ile Thr Pro Asp Lys Gly Arg Leu Ser Pro Glu Glu Ile Glu 530 535 540 Arg Met Ile Lys Asp Ala Glu Met Asn Ala Glu Lys Asp Lys Glu Val 545 550 555 560 Phe Asn Arg Val Gln Ala Arg Gln Ala Leu Glu Gly Tyr Ile Asp Ser 565 570 575 Met Thr Lys Thr Ile Asn Asp Asp Lys Thr Gly Lys Lys Leu Glu Asp 580 585 590 Asp Glu Lys Glu Lys Ile Arg Asp Ala Leu Asp Glu Gly Thr Lys Trp 595 600 605 Leu Ala Ser Asn Pro Glu Val Gly Ala Asp Glu Ile Ser Ala Lys Gln 610 615 620 His Glu Ile Glu Ala Ile Cys Asn Pro Ile Ile Ser Lys Leu Tyr Gly 625 630 635 640 Ser Gly Glu Asp Ser Asp Asp Ser Gly Tyr Ser Asp Glu Leu 645 650 <210> 39 <211> 400 <212> PRT <213> babesia duncani <400> 39 Met Ala Ile Pro Asp Asn Asn Asn Asn Thr Gln Ser Asn Gly Phe Asp 1 5 10 15 Thr Leu Glu Ser Asn Tyr Asp Glu Val Val Asp Ser Phe Glu Ala Leu 20 25 30 Lys Leu Asn Glu Asp Leu Leu Arg Gly Ile Tyr Ser Tyr Gly Phe Glu 35 40 45 Arg Pro Ser Ala Ile Gln Gln Arg Gly Ile Lys Pro Ile Ile Glu Asn 50 55 60 Tyr Asp Thr Ile Gly Gln Ala Gln Ser Gly Thr Gly Lys Thr Ala Thr 65 70 75 80 Phe Ser Ile Ala Ala Leu Gln Ile Ile Asn Tyr Asn Ile Met Ser Cys 85 90 95 Gln Thr Leu Ile Leu Ala Pro Thr Arg Glu Leu Ala Gln Gln Ile Gln 100 105 110 Lys Val Val Leu Ala Leu Gly Asp Tyr Leu Lys Val Gln Cys His Ala 115 120 125 Cys Val Gly Gly Thr Val Val Arg Asp Asp Ile His Lys Leu Lys Ala 130 135 140 Gly Val His Met Val Val Gly Thr Pro Gly Arg Val Tyr Asp Met Ile 145 150 155 160 Asp Lys Lys Ala Leu Leu Thr Asp Lys Ile Arg Leu Phe Ile Leu Asp 165 170 175 Glu Ala Asp Glu Met Leu Ser Arg Gly Phe Lys Gly Gln Ile His Glu 180 185 190 Val Phe Lys Arg Met Pro Pro Asp Val Gln Val Ala Leu Phe Ser Ala 195 200 205 Thr Met Pro Asn Glu Ile Leu Glu Leu Thr Thr Lys Phe Met Arg Ser 210 215 220 Pro Lys Leu Ile Leu Val Lys Lys Asp Glu Leu Thr Leu Glu Gly Ile 225 230 235 240 Lys Gln Phe Phe Val Met Ile Asp Lys Glu Asp Tyr Lys Phe Asp Thr 245 250 255 Leu Cys Asp Leu Tyr Glu Ser Val Thr Ile Thr Gln Ala Ile Ile Tyr 260 265 270 Cys Asn Thr Arg Arg Lys Val Asp Met Leu Thr Asn Lys Met Gln Glu 275 280 285 Lys Asp Phe Thr Val Ser Ser Met His Gly Asp Met Gly Gln Lys Glu 290 295 300 Arg Asp Leu Ile Met Arg Glu Phe Arg Ser Gly Ser Thr Arg Val Leu 305 310 315 320 Ile Thr Thr Asp Leu Leu Ala Arg Gly Ile Asp Val Gln Gln Val Ser 325 330 335 Leu Val Ile Asn Tyr Asp Leu Pro Met Ser Pro Asp Asn Tyr Ile His 340 345 350 Arg Ile Gly Arg Ser Gly Arg Phe Gly Arg Lys Gly Val Ala Ile Asn 355 360 365 Phe Leu Thr Pro Leu Asp Met Asp Ala Met Lys Ser Ile Glu Asn Tyr 370 375 380 Tyr Asn Thr Gln Ile Glu Glu Met Pro Ala Asp Ile Ala Ala Tyr Met 385 390 395 400 <210> 40 <211> 108 <212> PRT <213> babesia duncani <400> 40 Met Ser Lys Lys Leu Lys Thr Lys Gly Pro Glu Asn Ile Asn His Ser 1 5 10 15 Leu Gln Leu Val Met Lys Ser Gly Lys Val Cys Leu Gly Phe Lys Ser 20 25 30 Thr Arg Ala Ala Leu Arg Ser Gly Lys Ala Trp Met Ile Ile Leu Ser 35 40 45 Asn Asn Ile Pro Ala Leu Arg Arg Ser Glu Ile Glu Tyr Tyr Ala Met 50 55 60 Leu Ala Lys Cys Ser Val Tyr Arg Tyr Ser Gly Asp Asn Asn Asp Leu 65 70 75 80 Gly Thr Ala Cys Gly Lys Tyr Phe Arg Val Gly Cys Met Ala Val Leu 85 90 95 Asp Ala Gly Asp Ser Asp Ile Leu Arg Asn Ile Glu 100 105 <210> 41 <211> 418 <212> PRT <213> babesia duncani <400> 41 Met Thr Ser Val Asn Ser Asp Val Asp Ile Ser Glu Val Ser Gln Met 1 5 10 15 Ser Asp Ala Asp Ile Arg Val Arg Ile Asn Leu Ile Asp Ser Glu Ile 20 25 30 Lys Ile Leu Arg Ser Glu His Thr Arg Leu Lys Ser Arg Gln Lys Thr 35 40 45 Leu Gln Asp Arg Ile Lys Asp Asn Leu Glu Lys Ile Gln Leu Asn Lys 50 55 60 Gln Leu Pro Tyr Leu Val Ala Asn Val Val Glu Leu Leu Asp Phe Thr 65 70 75 80 Ser Asp Asp Glu Gln Asp Asp Gly Leu Thr Pro Ser Pro Ser Gln Lys 85 90 95 Lys Ser Lys Ser Leu Val Ile Lys Thr Ser Thr Arg Gln Thr Ile Phe 100 105 110 Leu Pro Val Ile Gly Leu Ile Pro Ala Ser Glu Leu His Pro Gly Glu 115 120 125 Leu Val Gly Val Asn Lys Asp Ser Tyr Leu Val Leu Asp Lys Leu Pro 130 135 140 Pro Glu Tyr Asp Asn Arg Val Lys Ala Met Glu Val Cys Glu Lys Pro 145 150 155 160 Ile Glu Asp Tyr Ser Asp Val Gly Gly Leu Asp Lys Gln Ile Gln Glu 165 170 175 Leu Val Glu Ala Ile Val Leu Pro Ile Thr His Gln Glu Arg Phe Lys 180 185 190 Lys Ile Gly Ile Lys Pro Pro Lys Gly Val Leu Met His Gly Pro Pro 195 200 205 Gly Thr Gly Lys Thr Leu Leu Ala Arg Ala Cys Ala Ala Gln Thr Lys 210 215 220 Ala Thr Phe Leu Lys Leu Ala Gly Pro Gln Leu Val Gln Met Phe Ile 225 230 235 240 Gly Asp Gly Ala Lys Met Val Arg Asp Ala Phe Ser Leu Ala Lys Glu 245 250 255 Lys Ala Pro Thr Ile Ile Phe Ile Asp Glu Ile Asp Ala Ile Gly Thr 260 265 270 Lys Arg Phe Asp Ser Glu Leu Ser Gly Asp Arg Glu Val Gln Arg Thr 275 280 285 Met Leu Glu Leu Leu Asn Gln Leu Asp Gly Phe Ala Ser Asp Asp Arg 290 295 300 Val Lys Val Ile Ala Ala Thr Asn Arg Pro Asp Thr Leu Asp Pro Ala 305 310 315 320 Leu Leu Arg Ser Gly Arg Leu Asp Arg Lys Ile Glu Leu Pro His Pro 325 330 335 Asn Glu Gln Ala Arg Cys His Ile Leu Gln Ile His Ser Arg Arg Met 340 345 350 Asn Val Asn Pro Asp Val Asn Phe Lys Glu Leu Ala Arg Ser Thr Asp 355 360 365 Asp Phe Asn Gly Ala Gln Leu Lys Ala Val Cys Ile Glu Ala Gly Met 370 375 380 Val Ala Leu Arg Arg Asp Ala Ser Glu Leu Glu His Glu Asp Phe Val 385 390 395 400 Glu Gly Ile Ser Met Val Gln Ala Lys Lys Lys Asn Thr Leu Asn Tyr 405 410 415 Leo Asn <210> 42 <211> 524 <212> PRT <213> babesia duncani <400> 42 Met Ala Gly His Ala Ala Leu Ile Leu Asn Phe Gly Ser Cys Phe Ser 1 5 10 15 Gly Val Leu Val Arg Leu Val Arg Asp Val Gly Ile Asn Cys Val Leu 20 25 30 Glu Ser Ala Glu Lys Ala Leu Asp Ala Leu Asn Thr Asn Ser Thr Val 35 40 45 Lys Val Ala Ile Leu Cys Gly Gly Leu Asp Ser Val Tyr Asp Glu Thr 50 55 60 Ser Leu Thr Val Pro Glu Glu Phe Ile Lys Ala Cys Glu Glu Lys Asn 65 70 75 80 Val Lys Ile Leu Ala Ile Ser His Ala Phe Tyr Ala Leu Cys Lys Thr 85 90 95 Leu Gly Ala Arg Leu Met Asn Gly Lys Gly Asn Asp Tyr Ile Ile Asp 100 105 110 Thr Val Thr Val Gln Arg Pro Met Val Leu Phe Asn Asn Val Gly Lys 115 120 125 His Phe Lys Ala Lys Ile Asn Pro Ile Asn Gly Val Glu Val Leu Pro 130 135 140 Ala Gly Phe Glu Ser Leu Ala Thr Phe Gly Asn Gly His Tyr Ala Ala 145 150 155 160 Ile Gly Asp Glu Lys Arg Gly Ile Phe Gly Val Ala Phe His Pro Glu 165 170 175 Ser Asp Asp Thr Glu Asn Gly Leu Val Ile Leu Lys Asn Phe Cys Leu 180 185 190 Glu Gln Gly Ala Cys Pro Ile Glu Trp Ser Met Glu Gln Tyr Leu Lys 195 200 205 Asp Glu Leu Ala Arg Cys Ile Ala Gln Cys Gly Asp Thr Lys Val Val 210 215 220 Val Ala Gly Leu Ser Gly Gly Val Asp Ser Thr Val Cys Ala Ala Ile 225 230 235 240 Val His Lys Ala Ile Gly Asn Arg Phe His Gly Val Met Ile Asn Thr 245 250 255 Gly Leu Met Arg Leu Asp Glu Thr Lys Lys Cys Ala Glu Arg Leu Lys 260 265 270 Lys Glu Ile Pro Gly Ile Gln Leu His Ile Arg Glu Ser Ala Asp Val 275 280 285 Phe Phe Gly Glu Leu Lys Gly Ile Leu Asp Pro Glu Gln Lys Arg Lys 290 295 300 Ile Ile Gly Lys Val Tyr Ile Asp Glu Phe Glu Arg Ala Ile Lys Asp 305 310 315 320 Leu Gly Phe Asp Lys Ser Asn Cys Leu Leu Leu Gln Gly Thr Ile Tyr 325 330 335 Pro Asp Ile Leu Glu Ser Glu Leu Asn Arg Arg Asn Gln Met Pro Ile 340 345 350 Lys Ser His His Asn Val Gly Gly Leu Pro Lys Asp Leu Ala Leu Glu 355 360 365 Leu Ile Glu Pro Val Arg Leu Leu Phe Lys Glu Glu Val Arg Lys Leu 370 375 380 Gly Arg Leu Leu Gly Leu Ser Gln Glu Ser Cys Glu Arg Gln Pro Phe 385 390 395 400 Pro Gly Pro Gly Leu Gly Val Arg Val Ile Gly Glu Leu Asn Pro Arg 405 410 415 Asn Leu Asp Leu Val Arg Arg Ala Asp Ala Val Met Asn Gln Ile Leu 420 425 430 Asp Ala Arg Gly Tyr Arg Ser Lys Ile Ser Gln Ser Gly Cys Ile Leu 435 440 445 Leu Ala Asp Val His Asn Thr Gly Ile Arg Asn Ser Gly Arg Thr Tyr 450 455 460 Gly His Ala Val Ile Ile Arg Ile Ile Ile Thr Thr Asp Phe Val Thr 465 470 475 480 Ala Gln Trp Ala Arg Ile Ile Asp Thr Asp Cys Leu Ala Glu Ile Ser 485 490 495 Lys Thr Ile Thr Asp Thr Val Pro Glu Ile Thr Arg Val Cys Tyr Asp 500 505 510 Ile Thr Asp Lys Pro Pro Ala Cys Ile Glu Trp Glu 515 520 <210> 43 <211> 211 <212> PRT <213> babesia duncani <400> 43 Met Ala Glu Glu Met Pro Gln Phe Lys Leu Leu Leu Val Gly Asp Gly 1 5 10 15 Gly Val Gly Lys Thr Thr Leu Val Lys Arg His Leu Thr Gly Glu Phe 20 25 30 Glu Lys Lys Tyr Ile Pro Thr Leu Gly Val Glu Val His Pro Leu Lys 35 40 45 Phe Arg Thr Asn Cys Gly Gly Ile Gln Phe Asn Ala Trp Asp Thr Ala 50 55 60 Gly Gln Glu Lys Tyr Gly Gly Leu Arg Asp Gly Tyr Tyr Ile Lys Gly 65 70 75 80 Glu Cys Ala Ile Ile Met Phe Asp Val Thr Ser Arg Ile Thr Tyr Arg 85 90 95 Asn Val Pro Asn Trp His Arg Asp Ile Val Arg Val Cys Glu Asn Ile 100 105 110 Pro Met Val Leu Val Gly Asn Lys Ala Asp Val Lys Glu Arg Gln Val 115 120 125 Lys Ala Gly His Ile Gln Phe His Arg Lys Arg Asn Leu Gln Tyr Tyr 130 135 140 Asp Leu Ser Ala Arg Ser Asn Phe Asn Phe Glu Arg Pro Phe Leu Trp 145 150 155 160 Leu Ser Arg Arg Leu Leu Asn Gln Pro Gln Leu Val Phe Val Gly Glu 165 170 175 Cys Ala Lys Ala Pro Glu Ile Gln Ile Asp Pro Leu Leu Ala Gln Gln 180 185 190 Ser Glu Arg Asp Leu Glu Ala Ala Ala Arg Val Ala Ile Asp Asp Asp 195 200 205 Gly Asp Leu 210 <210> 44 <211> 612 <212> PRT <213> babesia duncani <400> 44 Met Ala Asp Arg Phe Thr Gly Arg Asn Asn Arg Glu Ala Val Val Ala 1 5 10 15 Tyr Pro Gly Trp Phe Ser Glu Thr Gln Lys Gln Cys Leu Arg Ala Cys 20 25 30 Val Thr Ala Ser Gly Leu Ser Cys Leu Arg Val Ile Ser His Val His 35 40 45 Ala Met Ala Met Asp Tyr Gly Val Tyr Arg Val Lys Gln Leu Asn Asp 50 55 60 Glu Thr Pro Thr Arg Val Ala Leu Val Met Ile Gly His Cys His Ala 65 70 75 80 Ser Ala Ala Ile Val Asp Phe Tyr Ala Ser His Cys Ser Ile Leu Ser 85 90 95 Gln Val Ser Arg Arg Asn Leu Gly Gly Arg Asn Leu Asp Met Met Leu 100 105 110 Met Lys Tyr Met Ala Thr Glu Phe Ser Lys Lys Tyr His Cys Asp Pro 115 120 125 Leu Glu Asn Asn Lys Thr Arg Leu Lys Val Glu Ala Val Ala Val Lys 130 135 140 Thr Arg Arg Val Leu Ser Ala Asn Ala Glu Ser Ser Tyr Ser Ala Glu 145 150 155 160 Cys Leu Met Glu Asp Asn Asp Met Ser Gly His Ile Thr Arg Thr Gln 165 170 175 Phe Glu Glu Met Cys Asn Ala Glu Phe Ile Pro Gln Leu Ile Glu Met 180 185 190 Leu Lys Glu Cys Ile Glu Ala Ser Arg Thr Asp Leu Asp Ser Ile Phe 195 200 205 Ser Val Glu Ile Ala Gly Gly Ser Ser Arg Ile Pro Cys Ile Gln Gln 210 215 220 Ala Ile Ser Ser Ile Phe Asn Lys Val Pro Ser Arg Thr Leu Asn Ala 225 230 235 240 Asp Glu Cys Ile Ala Arg Gly Cys Val Leu Glu Ala Ala Ile Lys Ser 245 250 255 Asn His Tyr Arg Val Arg Glu Tyr Lys Thr Arg Leu Thr Leu Pro Arg 260 265 270 Ser Leu Thr Leu Gly Tyr Phe Asn Gly Gln Glu Pro Met Leu Leu Glu 275 280 285 Ala Ile Ala Ala Gly Thr Pro Leu Gly Asp Pro Ile Arg Val Thr Leu 290 295 300 Gln Ala Gln Ala Pro Val Cys Val Arg Val Ala Leu Gly Asp Ala Leu 305 310 315 320 Asp Pro Arg Ser Gln Asp Ala Leu Gly Thr Leu Asp Ile Ala Arg His 325 330 335 Ile Ser Gln Glu Ala Gln Pro Ala Pro Val Thr Thr Asn Asp Gly Ala 340 345 350 Ala Ile Gln Thr Asp Glu Gln Asp Ala Glu Ile Gln Ser Glu Ser Ser 355 360 365 Pro Ser Gly Gly Ile Ser Val Thr Leu Gly Phe Asp Asp Cys Gly Gln 370 375 380 Phe Val Ala Ser Pro Glu Cys Cys Glu Tyr Arg Trp Leu Pro Ala Thr 385 390 395 400 Ile Leu Asp Ile Ala Arg Leu Glu Ala Ala Glu Leu Glu Ala Arg Gly 405 410 415 Arg Asp Leu Lys Glu Asn Ser Arg Leu Gln Ala Leu Asn Asp Phe Glu 420 425 430 Thr Leu Leu Tyr Thr Val Arg Asp Lys Met Gln Ser Ser His Arg Asp 435 440 445 Phe Ile Asp Pro Gln Met Ile Pro Ala Tyr Glu Ser Glu Leu Asp His 450 455 460 Trp Arg Glu Trp Leu Tyr Glu Asn Ser Gly Ala Ser Gln Glu Thr Leu 465 470 475 480 Gln Glu Gly Ile Asp Lys Val Ser Ser Glu Trp Lys Arg Ile Asp Lys 485 490 495 Tyr Phe Lys Glu His Gln Asn Lys Leu Glu Asn Leu Glu Pro Phe Leu 500 505 510 Gln Arg Leu Gln Glu Arg Tyr Asn Phe Cys Cys Glu Asp Asn Asn Pro 515 520 525 Asn Trp His Gly Ala Thr Pro Glu Glu Arg Leu Asn Phe Ala Gln Glu 530 535 540 Leu Met Asp Leu Asp Ser Arg Val Arg Gln Met His Gln Asp Glu Ser 545 550 555 560 Gln Arg Pro Arg His Met Glu Pro Leu Phe Thr Met Gln Gln Ile Gln 565 570 575 Gly Glu Met Gln Lys Leu Leu Val Ser Ile Ser Glu Phe Cys Gln Ala 580 585 590 Lys Ala Ala Lys Ala Pro Ala Gln Glu Pro Pro Glu Gln Gln Pro Lys 595 600 605 Glu Gln Gln Glu 610 <210> 45 <211> 152 <212> PRT <213> babesia duncani <400> 45 Met Asp Ala Gly Gly Lys Ile Gly Gly Lys Ile Gly Gly Lys Val Gly 1 5 10 15 Gly Met Gly Lys Gly Gly Lys Gly Lys Thr Gly Ser Gly Lys Gly Lys 20 25 30 Lys Ala Pro Met Ser Arg Ala Ala Arg Ala Gly Leu Gln Phe Pro Val 35 40 45 Gly Arg Val His Arg Met Leu Lys Ser Arg Ile Ser Ala Asp Gly Arg 50 55 60 Val Gly Ser Thr Ala Ala Val Tyr Ala Ser Ala Ile Leu Glu Tyr Leu 65 70 75 80 Thr Ala Glu Val Leu Glu Leu Ala Gly Asn Ala Ser Lys Asp Leu Lys 85 90 95 Val Lys Arg Ile Thr Pro Arg His Leu Gln Leu Ala Ile Arg Gly Asp 100 105 110 Glu Glu Leu Asp Thr Leu Ile Lys Ala Thr Ile Ala Gly Gly Gly Val 115 120 125 Ile Pro His Ile His Lys Ala Leu Met Asn Lys Gly Pro Ala Gln Val 130 135 140 Leu Val Lys Pro Pro Lys Arg Ile 145 150 <210> 46 <211> 396 <212> PRT <213> babesia duncani <400> 46 Met Gly Ile Val Thr Ala Ser Ile Ala Pro Leu His Ile Gly Asp Asp 1 5 10 15 Leu Tyr Thr Arg Met Lys Thr Leu Glu Lys Lys Leu Glu Ile Cys Glu 20 25 30 Ile Gln Glu Asn Tyr Val Arg Glu Glu Tyr Arg Asn Leu Lys Leu Glu 35 40 45 Leu Ile Arg Ala Arg Glu Glu Ile Lys Arg Ile Gln Ser Val Pro Leu 50 55 60 Val Ile Gly Gln Phe Leu Asp Met Ile Asp Lys Asn Tyr Gly Ile Val 65 70 75 80 Ser Ser Thr Ala Gly Ser Asn Tyr Tyr Val Arg Ile Leu Ser Thr Ile 85 90 95 Asn Arg Glu Leu Leu Thr Pro Asn Ser Ser Val Ala Leu His Arg His 100 105 110 Ser His Ser Val Val Asp Leu Leu Pro Pro Glu Ala Asp Ser Ser Ile 115 120 125 Gln Leu Met Gln Val Ser Glu Lys Pro Asp Val Thr Tyr Ala Asp Ile 130 135 140 Gly Gly Leu Asp Ile Gln Lys Gln Glu Ile Arg Glu Ala Val Glu Leu 145 150 155 160 Pro Leu Thr Cys Pro Glu Leu Tyr Arg Gln Ile Gly Ile Asp Pro Pro 165 170 175 Val Gly Val Leu Leu Tyr Gly Pro Pro Gly Thr Gly Lys Thr Met Leu 180 185 190 Ala Lys Ala Val Ala Asn Gln Thr Asp Ala Lys Phe Ile Arg Val Val 195 200 205 Gly Ser Glu Phe Val Gln Lys Tyr Leu Gly Glu Gly Pro Arg Met Val 210 215 220 Arg Asp Ile Phe Arg Leu Ala Arg Glu Asn Ala Pro Ala Ile Leu Phe 225 230 235 240 Ile Asp Glu Val Asp Ala Ile Ala Thr Lys Arg Phe Asp Ala Gln Thr 245 250 255 Gly Ala Asp Arg Glu Val Gln Arg Ile Leu Leu Glu Leu Leu Asn Gln 260 265 270 Met Asp Gly Phe Asp Gln Asn Ala Thr Val Lys Val Ile Met Ala Thr 275 280 285 Asn Arg Ala Asp Thr Leu Asp Pro Ala Leu Leu Arg Pro Gly Arg Leu 290 295 300 Asp Arg Lys Ile Glu Phe Pro Leu Pro Asp Arg Arg Gln Arg Arg Leu 305 310 315 320 Ile Phe Gln Thr Ile Thr Ser Asn Met Asn Leu Ala Ala Asp Val Asp 325 330 335 Leu Glu Thr Phe Val Ala Arg Pro Glu Lys Val Ser Ala Ala Asp Ile 340 345 350 Ala Ala Ile Cys Gln Glu Ala Gly Ile Gln Ala Ile Arg Lys Asn Arg 355 360 365 Tyr Val Val Thr Thr Lys Asp Phe Glu Arg Gly Trp Lys Arg His Ile 370 375 380 Arg Lys His Glu Arg Asp Tyr Gly Phe Tyr Gly Val 385 390 395 <210> 47 <211> 712 <212> PRT <213> babesia microti <400> 47 Met Ser Ser Gln Glu Thr Phe Glu Phe Asn Ala Asp Ile Ser Gln Leu 1 5 10 15 Leu Ser Leu Ile Ile Asn Ala Phe Tyr Ser Asn Lys Glu Ile Phe Leu 20 25 30 Arg Glu Leu Ile Ser Asn Ala Ser Asp Ala Leu Glu Lys Ile Arg Tyr 35 40 45 Glu Leu Leu Arg Asp Gly Thr Lys Val Ser Asp Glu Ser Glu Phe Ser 50 55 60 Ile Lys Ile Ser Ala Asp Lys Ser Asn Asn Thr Leu Thr Ile Glu Asp 65 70 75 80 Ser Gly Ile Gly Met Thr Lys Ala Asp Leu Ile Asn Asn Leu Gly Thr 85 90 95 Ile Ala Lys Ser Gly Thr Lys Ala Phe Met Glu Ala Met Gln Ser Gly 100 105 110 Cys Asp Met Ser Met Ile Gly Gln Phe Gly Val Gly Phe Tyr Ser Ala 115 120 125 Tyr Leu Val Ala Glu Lys Val Thr Val Val Ser Lys His Asn Ser Asp 130 135 140 Glu Gln Tyr Ile Trp Glu Ser Ser Ala Ser Gly Val Phe Thr Ile Thr 145 150 155 160 Lys Asp Glu Thr Thr Glu Lys Met Lys Arg Gly Thr Arg Leu Ile Leu 165 170 175 Gln Leu Lys Glu Asp Gln Thr Glu Tyr Leu Glu Glu Arg Arg Leu Lys 180 185 190 Glu Leu Val Lys Lys His Ser Glu Phe Ile Ser Phe Pro Ile His Leu 195 200 205 Leu Cys Glu Lys Thr Lys Glu Glu Glu Val Thr Ala Ser Asp Asp Glu 210 215 220 Gly Asp Lys Lys Glu Asp Asp Lys Lys Glu Asp Asp Glu Lys Glu Asp 225 230 235 240 Asp Lys Lys Gly Glu Asp Glu Lys Val Glu Asp Val Ser Glu Asp Lys 245 250 255 Lys Lys Thr Lys Lys Val Ser Thr Val Thr Lys Glu Trp Glu Val Leu 260 265 270 Asn Lys Gln Lys Pro Ile Trp Met Arg Gln Pro Asn Glu Val Thr Asn 275 280 285 Glu Glu Tyr Ala Asn Phe Tyr Lys Asn Leu Thr Asn Asp Trp Glu Asp 290,295,300 His Leu Ala Val Lys His Phe Ser Val Glu Gly Gln Leu Glu Phe Arg 305 310 315 320 Ala Ile Leu Phe Ile Pro Lys Arg Ala Pro Phe Asp Met Phe Glu Asn 325 330 335 Arg Lys Lys Lys Asn Asn Ile Lys Leu Tyr Val Arg Val Phe Ile 340 345 350 Met Asp Asp Cys Glu Glu Leu Ile Pro Glu Trp Leu Ser Phe Val Lys 355 360 365 Gly Val Val Asp Ser Glu Asp Leu Pro Leu Asn Ile Ser Arg Glu Thr 370 375 380 Lion Gln Gln Asn Lys And Lion Lys And Arg Lys Donkey Lion Val Lys 385 390 395 400 Lys Cys Leu Glu Leu Phe Ser Glu Leu Thr Glu Lys Asp Asp Phe 405 410 415 Lys Phe Tyr Glu Gln Phe Asn Lys Asn Leu Lys Leu Gly Ile His 420 425 430 Glu Asp Ser Ala Asn Arg Asn Lys Ile Ser Glu Leu Leu Arg Phe Glu 435 440 445 Thr Thr Lys Ser Gly Asp Glu Ala Ile Ser Leu Arg Glu Tyr Val Asp 450 455 460 Arg Met Lys Pro Asn Gln Lys Tyr Ile Tyr Tyr Ile Thr Gly Glu Ser 465 470 475 480 Ile Gln Ala Val Ser Asn Ala Pro Phe Leu Glu Lys Leu Lys Asp Lys 485 490 495 Asn Ile Glu Val Ile Tyr Met Thr Asp Pro Ile Asp Glu Tyr Ala Val 500 505 510 Gln Gln Ile Lys Glu Phe Asp Gly Lys Lys Leu Arg Cys Cys Thr Lys 515 520 525 Glu Gly Leu Asp Ile Asp Asp Glu Lys Asp Glu Glu Glu Glu Lys Arg 530 535 540 Phe Glu Gln Val Lys Gln Glu Met Glu Pro Leu Cys Lys Thr Ile Lys 545 550 555 560 Glu Val Leu His Asp Lys Val Glu Lys Val Thr Cys Gly Lys Arg Phe 565 570 575 Thr Thr Ser Pro Leu Ala Leu Val Thr Ser Glu Phe Gly Trp Ser Ala 580 585 590 Asn Met Glu Arg Ile Met Arg Ala Gln Ala Leu Arg Asn Ser Ser Ile 595 600 605 Thr Ser Tyr Met Val Ser Lys Lys Thr Met Glu Ile Asn Pro Tyr His 610 615 620 Ser Ile Met Lys Ala Leu Lys Glu Arg Val Ala Ala Asp Lys Ser Asp 625 630 635 640 Lys Thr Val Lys Asp Leu Ile Trp Leu Leu Tyr Glu Ser Ala Leu Leu 645 650 655 Ile Ser Gly Phe Asn Leu Glu Glu Pro Thr Gln Phe Gly Asn Arg Ile 660 665 670 Phe Arg Met Ile Lys Leu Gly Leu Ala Leu Glu Asp Asp Gln Pro Asp 675 680 685 Asp Thr Asp Leu Pro Pro Leu Asp Glu Gly Val Ala Val Asp Gly Gly 690 695 700 Asp Ser Lys Met Glu Glu Val Asp 705 710 <210> 48 <211> 447 <212> PRT <213> babesia microti <400> 48 Met Pro Lys Glu Lys Thr His Ile Asn Leu Val Val Ile Gly His Val 1 5 10 15 Asp Ser Gly Lys Ser Thr Thr Thr Gly His Leu Ile Tyr Lys Leu Gly 20 25 30 Gly Ile Asp Lys Arg Thr Ile Glu Lys Phe Glu Lys Asp Ser Ser Glu 35 40 45 Met Gly Lys Ser Ser Phe Lys Tyr Ala Trp Val Leu Asp Lys Leu Lys 50 55 60 Ser Glu Arg Glu Arg Gly Ile Thr Ile Asp Ile Thr Leu Trp Lys Phe 65 70 75 80 Glu Thr Gln Lys Tyr Glu Tyr Thr Val Ile Asp Ala Pro Gly His Arg 85 90 95 Asp Phe Ile Lys Asn Met Ile Thr Gly Thr Ser Gln Ala Asp Val Ala 100 105 110 Met Leu Val Val Pro Ala Glu Ser Gly Gly Phe Glu Ala Ala Phe Ser 115 120 125 Lys Glu Gly Gln Thr Arg Glu His Ala Leu Leu Ala Phe Thr Leu Gly 130 135 140 Val Lys Gln Met Ile Val Ala Ile Asn Lys Met Asp Ser Cys Gln Tyr 145 150 155 160 Lys Glu Asp Arg Tyr Met Glu Ile Phe Lys Glu Val Gln Gln Tyr Leu 165 170 175 Lys Lys Val Gly Tyr Lys Val Glu Ser Val Pro Phe Val Ala Ile Ser 180 185 190 Gly Phe His Gly Asp Asn Met Val Glu Lys Ser Thr Asn Met Pro Trp 195 200 205 Tyr Lys Gly Lys Thr Leu Val Glu Ala Leu Asp Gln Met Glu Pro Pro 210 215 220 Lys Arg Pro Val Glu Lys Pro Leu Arg Leu Pro Leu Gln Ser Val Tyr 225 230 235 240 Lys Ile Gly Gly Ile Gly Thr Val Pro Val Gly Arg Val Glu Thr Gly 245 250 255 Gln Leu Lys Ala Gly Met Ile Ile Thr Phe Ala Pro Thr Gly Leu Thr 260 265 270 Thr Glu Cys Lys Ser Val Glu Met His His Glu Val Val Glu Val Ala 275 280 285 Ser Pro Gly Asp Asn Val Gly Phe Asn Val Lys Asn Val Ser Val Lys 290 295 300 Asp Ile Lys Arg Gly Asn Val Ala Ser Asp Ser Lys Asn Asp Pro Ala 305 310 315 320 Lys Glu Ala Thr Ser Phe Ser Ala Gln Val Ile Val Leu Asn His Pro 325 330 335 Gly Thr Ile Lys Ala Gly Tyr Ser Pro Val Val Asp Cys His Thr Ala 340 345 350 His Ile Ala Cys Lys Phe Glu Ser Leu Asp Thr Arg Ile Asp Lys Arg 355 360 365 Thr Gly Lys Thr Leu Glu Glu Asn Pro Lys Thr Ile Lys Asn Gly Asp 370 375 380 Ala Ala Met Val Thr Met Lys Pro Asn Lys Pro Met Val Val Glu Thr 385 390 395 400 Phe Thr Asp Tyr Ala Pro Leu Gly Arg Phe Ala Val Arg Asp Met Arg 405 410 415 Gln Thr Val Ala Val Gly Ile Ile Lys Ala Val Glu Lys Lys Asp Pro 420 425 430 Ser Ser Ala Lys Val Thr Lys Ser Ala Val Lys Ala Gly Lys Lys 435 440 445 <210> 49 <211> 438 <212> PRT <213> babesia microti <400> 49 Met Thr Lys Ile Ile Ser Ala Cys Gly Arg Glu Val Leu Asp Ser Arg 1 5 10 15 Gly Asn Pro Thr Val Glu Cys Glu Val Thr Thr Glu Gly Gly Lys Phe 20 25 30 Arg Ala Ile Val Pro Ser Gly Ala Ser Thr Gly Ile Tyr Glu Ala Leu 35 40 45 Glu Leu Arg Asp Gly Asp Lys Thr Arg Tyr Leu Gly Lys Gly Val Gln 50 55 60 Asn Ala Ile Lys Asn Met His Asn Ile Ile Cys Pro Gly Ile Gln Gly 65 70 75 80 Phe Leu Cys Thr Glu Gln Glu Lys Leu Asp Asn His Met Val Lys Val 85 90 95 Leu Asp Gly Thr Gln Asn Glu Trp Gly Phe Ser Lys Ser Lys Leu Gly 100 105 110 Ala Asn Thr Ile Leu Ala Val Ser Met Gly Ala Ala Arg Ala Gly Ala 115 120 125 Ala Ala Lys Gly Ile Pro Leu Tyr Glu His Leu Ala Gln Leu Ser Gly 130 135 140 Lys Pro Thr Asp Lys Phe Ile Met Pro Val Pro Cys Leu Asn Val Ile 145 150 155 160 Asn Gly Gly Ser His Ala Gly Asn Ala Leu Ala Phe Gln Glu Phe Met 165 170 175 Ile Leu Pro Thr Val Ala Asp Asn Phe Ser Asn Ala Leu Arg Met Gly 180 185 190 Val Glu Val Tyr His Thr Leu Lys Lys Val Ile Asn Lys Lys Tyr Gly 195 200 205 Gln Asp Ala Thr Asn Val Gly Asp Glu Gly Gly Phe Ala Pro Asn Ile 210 215 220 Ser Thr Pro Gln Glu Ala Leu Asp Leu Leu Val Glu Ala Ile Ala Ala 225 230 235 240 Ala Gly Tyr Thr Gly Lys Ile Lys Ile Ala Met Asp Val Ala Ala Ser 245 250 255 Glu Phe Tyr Gln Lys Asp Val Lys Met Tyr Asn Leu Thr Phe Lys Ser 260 265 270 Ser Ser Pro Asp Ile Lys Thr Ser Asp Gln Leu Val Glu Leu Tyr Lys 275 280 285 Glu Leu Val Asn Lys Tyr Pro Ile Val Ser Ile Glu Asp Pro Phe Asp 290 295 300 Gln Asp Asp Trp Glu Ala Tyr Ala Lys Leu Thr Ala Ala Ile Gly Asp 305 310 315 320 Lys Ile Gln Ile Val Gly Asp Asp Leu Leu Val Thr Asn Pro Lys Arg 325 330 335 Ile Glu Ala Ala Ile Gln Lys Lys Ala Cys Asn Ala Leu Leu Leu Lys 340 345 350 Val Asn Gln Ile Gly Ser Val Thr Glu Ser Ile Gln Ala Cys Lys Ile 355 360 365 Ser Gln Glu Asn Gly Trp Gly Val Met Val Ser His Arg Ser Gly Glu 370 375 380 Thr Glu Asp Val Phe Ile Ser Asp Leu Val Val Ala Leu Gly Thr Gly 385 390 395 400 Gln Ile Lys Thr Gly Ala Pro Cys Arg Ser Glu Arg Asn Ala Lys Tyr 405 410 415 Asn Gln Leu Leu Arg Ile Glu Gln Glu Leu Gly Glu Arg Ala Thr Tyr 420 425 430 Ser Lys Val Phe Asn Lys 435 <210> 50 <211> 77 <212> PRT <213> babesia microti <400> 50 Met Gln Ile Phe Val Lys Thr Leu Thr Gly Lys Thr Ile Thr Leu Glu 1 5 10 15 Val Glu Pro Ser Asp Thr Ile Glu Asn Val Lys Ala Lys Ile Gln Asp 20 25 30 Lys Glu Gly Ile Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys 35 40 45 Gln Leu Glu Asp Gly Arg Thr Leu Ser Asp Tyr Asn Ile Gln Lys Glu 50 55 60 Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly Asp 65 70 75 <210> 51 <211> 282 <212> PRT <213> babesia microti <400> 51 Met Gln Ile Phe Val Lys Thr Leu Thr Gly Lys Thr Ile Thr Leu Glu 1 5 10 15 Val Glu Pro Ser Asp Thr Ile Glu Asn Val Lys Ala Lys Ile Gln Asp 20 25 30 Lys Glu Gly Ile Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys 35 40 45 Gln Leu Glu Asp Gly Arg Thr Leu Ser Asp Tyr Asn Ile Gln Lys Glu 50 55 60 Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly Met Gln Ile Phe 65 70 75 80 Val Lys Thr Leu Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Pro Ser 85 90 95 Asp Thr Ile Glu Asn Val Lys Ala Lys Ile Gln Asp Lys Glu Gly Ile 100 105 110 Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp 115 120 125 Gly Arg Thr Leu Ser Asp Tyr Asn Ile Gln Lys Glu Ser Thr Leu His 130 135 140 Leu Val Leu Arg Leu Arg Gly Gly Met Gln Ile Phe Val Lys Thr Leu 145 150 155 160 Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Pro Ser Asp Thr Ile Glu 165 170 175 Asn Val Lys Ala Lys Ile Gln Asp Lys Glu Gly Ile Pro Pro Asp Gln 180 185 190 Gln Arg Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp Gly Arg Thr Leu 195 200 205 Ser Asp Tyr Asn Ile Gln Lys Glu Ser Thr Leu His Leu Val Leu Arg 210 215 220 Leu Arg Gly Gly Val Ile Asp Pro Ser Leu Ala Leu Leu Ala Gln Lys 225 230 235 240 Tyr Asn Cys Asn Lys Met Val Cys Arg Lys Cys Tyr Ala Arg Leu Pro 245 250 255 Pro Arg Ala Thr Asn Cys Arg Lys Lys Arg Cys Gly His Cys Asn Asp 260 265 270 Leu Arg Pro Lys Lys Lys Ile Lys Gly Asn 275 280 <210> 52 <211> 376 <212> PRT <213> babesia microti <400> 52 Met Gly Asp Asp Asp Asn Ala Ala Leu Val Val Asp Asn Gly Ser Gly 1 5 10 15 Asn Val Lys Ala Gly Ile Ala Gly Asp Asp Ala Pro Arg Cys Val Phe 20 25 30 Pro Ser Ile Val Gly Arg Pro Lys Asn Pro Ala Leu Met Ile Gly Met 35 40 45 Asp Glu Lys Glu Val Tyr Val Gly Asp Glu Ala Gln Ser Lys Arg Gly 50 55 60 Ile Leu Thr Leu Lys Tyr Pro Ile Glu His Gly Ile Val Thr Asn Trp 65 70 75 80 Asp Asp Met Glu Lys Ile Trp His His Thr Phe Tyr Asn Glu Leu Arg 85 90 95 Val Asn Pro Glu Glu His Ser Val Leu Leu Thr Glu Ala Pro Leu Asn 100 105 110 Pro Lys Thr Asn Arg Glu Lys Met Ala Thr Ile Met Phe Glu Thr His 115 120 125 Asn Val Pro Ala Met Tyr Val Ala Ile Gln Ala Val Leu Ser Leu Tyr 130 135 140 Ser Ser Gly Arg Thr Thr Gly Ile Val Leu Asp Ser Gly Asp Gly Val 145 150 155 160 Ser His Thr Val Pro Ile Tyr Glu Gly Tyr Ala Met Pro Ser Ala Ile 165 170 175 Met Arg Leu Asp Leu Ala Gly Arg Asp Leu Thr Glu Tyr Met Gln Lys 180 185 190 Ile Leu Val Glu Arg Gly Phe Ser Phe Thr Thr Ser Ala Glu Lys Glu 195 200 205 Ile Val Arg Asp Ile Lys Glu Lys Leu Cys Tyr Ile Ala Leu Asp Phe 210 215 220 Asp Glu Glu Met Gln Ala Ala Glu Thr Ser Ser Asp Leu Glu Lys Ser 225 230 235 240 Tyr Glu Leu Pro Asp Gly Asn Ile Ile Thr Val Gly Asn Glu Arg Phe 245 250 255 Arg Cys Ala Glu Val Leu Phe Gln Pro Ser Phe Ile Gly Lys Glu Cys 260 265 270 His Gly Leu His Lys Thr Thr Phe Asp Ser Ile Ile Lys Cys Asp Val 275 280 285 Asp Ile Arg Arg Asp Leu Tyr Ser Asn Val Val Leu Ser Gly Gly Thr 290 295 300 Thr Met Leu Gln Gly Ile Gly Glu Arg Leu Thr Lys Glu Leu Ser Cys 305 310 315 320 Leu Ala Pro Ser Thr Met Lys Ile Lys Val Val Ala Pro Pro Glu Arg 325 330 335 Lys Tyr Ser Val Trp Ile Gly Gly Ser Ile Leu Ser Ser Leu Ser Thr 340 345 350 Phe Gln Gln Met Trp Ile Thr Lys Asp Glu Phe Asp Glu Ser Gly Pro 355 360 365 Val Ile Val His Arg Lys Cys Phe 370 375 <210> 53 <211> 187 <212> PRT <213> babesia microti <400> 53 Met His Asn His Ser Tyr Tyr Thr Ile Leu Leu Thr Ile Ala Leu Ile 1 5 10 15 His Thr Thr Gly Cys His Gly Phe Leu His Arg Asn Ile Lys Phe Ile 20 25 30 Leu His Ser Met Thr Val Tyr Gly Lys Pro Lys Arg Leu His Lys Thr 35 40 45 Pro Pro Trp Ala His Leu Phe Glu Glu Lys Val Glu Pro Ser Pro Leu 50 55 60 Gly Glu Pro Trp Ala Lys Leu Ser Lys Asp Val Ala Asn Gly Glu Arg 65 70 75 80 Arg Val Arg Leu Thr Val Lys Lys Ser His Leu Gln Ile Tyr Ala Ala 85 90 95 Val Val Asp Asp Tyr Lys Asn Gln Val Ile Cys Ile Ala Ser Ser Asn 100 105 110 Leu Pro Val Leu Ala Asp Val Leu Gly Thr Val Pro Thr Lys Asp Pro 115 120 125 Thr Val Arg Arg Asn Lys Gly Asn Asn Val Lys Ala Ala Tyr Glu Val 130 135 140 Gly Lys His Ile Gly Arg Leu Ala Leu Ala Lys Gly Val Ala Lys Val 145 150 155 160 Tyr Phe Asp Arg Ala Gly Tyr Lys Tyr His Gly Arg Val Glu Ala Val 165 170 175 Ala Ile Gly Ala Arg Lys Val Gly Leu Gln Leu 180 185 <210> 54 <211> 425 <212> PRT <213> babesia microti <400> 54 Met Tyr Gln Ile Asp Arg Met Ile Asp Lys His Lys Asp Pro Ile Asp 1 5 10 15 Pro Leu Gln Thr Ile Leu Ser Val Lys Gly Thr Met Lys Cys Lys Leu 20 25 30 Ser Glu Met Leu Thr Arg His Ser Thr Glu Asp Arg His Ser Leu Ser 35 40 45 Leu Val Ala Asp Leu Lys Arg Glu Ser Pro Thr His Thr Asp Ser Arg 50 55 60 Ser Gly Val Arg Leu Ser Phe Leu Asp Ala Gly Glu Val Val Val Thr 65 70 75 80 Met Ala Asn Thr Gly Phe Asp Val Val Leu Val Asn Thr Asp Asp Ile 85 90 95 Ala Tyr Lys Gly Thr Leu Asp Asp Leu Lys Thr Ser Ile Cys Ala Ala 100 105 110 His Ala Ile Gly Asn Arg Ser Arg Pro Ala Val Val Met Lys Asp Ile 115 120 125 Ile Leu His Pro Leu Gln Leu Ala Gln Ala Ala Gln Leu His Ala Asp 130 135 140 Gly Val Val Leu Asn Ser Phe Tyr Leu Gly Pro Ala Leu Glu Ser Met 145 150 155 160 Ile Asp Thr Ser Tyr Asn Leu Gly Ile Glu Pro Ile Val Glu Val His 165 170 175 Thr Leu Glu Asp Ala Leu Tyr Ala Ile Gln Leu His Thr Lys Ile Leu 180 185 190 Met Ile Asn Gln Trp Asp Arg Leu Thr Asn Lys Cys His Pro Asn Arg 195 200 205 Ala Leu Gln Ile Arg Glu Ile Val Pro Asp Gly Ile Ile Thr Ile Ala 210 215 220 Cys Gly Gly Ile Lys Thr Leu Glu Gln Ile Glu Gln Leu Gly Leu Ala 225 230 235 240 Gly Tyr Asp Ala Val Val Leu Gly Lys Lys Leu Ala Asp Thr Asn Ile 245 250 255 Pro Ser Phe Val Gly Ser Ile Lys Lys Trp Asn Ala Pro Gly Lys Gly 260 265 270 Ile Leu Ala Ile Ser Lys Pro Leu Phe Phe Thr Asp Glu Met Asp Glu 275 280 285 Lys Asp Val Ser Gly Gly Gly His Val Ile Arg Met Lys Gln Asn Tyr 290 295 300 Arg Gln Thr Leu Gln Glu Met Cys Glu Phe Tyr Gln Ile Ala Glu Asn 305 310 315 320 Asn Cys Val Glu Ala Pro Arg Pro Lys Asp Val Leu Leu Arg Phe Ile 325 330 335 Gly Asn Asp Met Pro Glu Lys Trp Ile Phe Lys Arg Glu Lys Trp Met 340 345 350 Lys Asp His Ala His Glu Tyr Pro Ser Glu Asp His Ala Thr Ala Val 355 360 365 Tyr Asp Phe Asn Leu Ala Val Glu Leu Asn Thr Thr Leu Glu Cys Asn 370 375 380 Lys Lys Leu Leu Ser Gln His Phe Lys Arg Glu Met Val Asp Lys Leu 385 390 395 400 Glu Glu Ala Ile Lys Asn Tyr Val Lys Lys Cys Tyr Ile Asn Leu Lys 405 410 415 Arg Phe Thr Asn Lys Ile Ser Cys Ser 420 425 <210> 55 <211> 644 <212> PRT <213> babesia microti <400> 55 Met Ser Gln Gly Pro Ala Ile Gly Ile Asp Leu Gly Thr Thr Tyr Ser 1 5 10 15 Cys Val Gly Val Trp Lys Asn Glu Thr Val Glu Ile Ile Ala Asn Asp 20 25 30 Gln Gly Asn Arg Thr Thr Pro Ser Tyr Val Ala Phe Thr Asp Val Glu 35 40 45 Arg Leu Val Gly Asp Ala Ala Lys Asn Gln Asp Ala Arg Asn Pro Glu 50 55 60 Asn Thr Val Phe Asp Ala Lys Arg Leu Ile Gly Arg Lys Ile Asn Asp 65 70 75 80 Pro Cys Ile Gln Ser Asp Ile Lys His Trp Pro Phe Thr Val Ala Ala 85 90 95 Gly Pro Asn Asp Lys Pro Val Ile Lys Val Gln Phe Gln Gly Glu Thr 100 105 110 Lys Ser Phe His Pro Glu Glu Ile Ser Ser Met Val Leu Thr Lys Met 115 120 125 Lys Glu Ile Ala Glu Ser Tyr Leu Gly Lys Thr Ile Ser Asn Ala Val 130 135 140 Ile Thr Val Pro Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ala Thr Lys 145 150 155 160 Asp Ala Gly Thr Ile Ala Gly Leu Asn Val Met Arg Ile Ile Asn Glu 165 170 175 Pro Thr Ala Ala Ala Ile Ala Tyr Gly Met Asp Lys Lys Gly Thr Ser 180 185 190 Glu Lys Asn Val Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe Asp Val 195 200 205 Ser Ile Leu Thr Ile Glu Asp Gly Ile Phe Glu Val Lys Ala Thr Gln 210 215 220 Gly Asp Thr His Leu Gly Gly Glu Asp Phe Asp Asn Arg Leu Val Asn 225 230 235 240 Phe Cys Val Asp Asp Phe Lys Arg Lys Asn Gly Gly Lys Asn Ile Ser 245 250 255 Thr Asn Arg Arg Ala Leu Arg Arg Leu Arg Thr Gln Cys Glu Arg Ala 260 265 270 Lys Arg Thr Leu Ser His Ser Thr Gln Ala Thr Ile Val Val Glu Ala 275 280 285 Ile Phe Asp Gly Ile Asp Tyr Ser Cys Asn Ile Thr Arg Ala Arg Phe 290 295 300 Glu Glu Leu Cys Ala Glu Met Phe Lys Asn Thr Leu Ile Pro Val Glu 305 310 315 320 Lys Ala Leu Ala Asp Ala Asp Met Asp Lys Lys Gln Ile His Glu Val 325 330 335 Val Leu Val Gly Gly Ser Thr Arg Ile Pro Lys Ile Gln Gln Leu Ile 340 345 350 Lys Asp Phe Phe Asn Gly Lys Glu Pro Cys Lys Ser Ile Asn Pro Asp 355 360 365 Glu Ala Val Ala Tyr Gly Ala Ala Val Gln Ala Ala Ile Leu Thr Gly 370 375 380 Glu Gln Ser Ser Lys Val Gln Asp Leu Leu Leu Leu Asp Val Thr Pro 385 390 395 400 Leu Ser Leu Gly Leu Glu Thr Ala Gly Gly Val Met Thr Val Leu Ile 405 410 415 Pro Arg Asn Thr Thr Ile Pro Ala Lys Lys Glu Gln Glu Phe Thr Thr 420 425 430 Asn Glu Asn Asn Gln Thr Gly Val Met Ile Gln Val Phe Glu Gly Glu 435 440 445 Arg Ser Met Thr Cys Asp Asn Asn Leu Leu Gly Lys Phe His Leu Thr 450 455 460 Gly Ile Pro Pro Ala Pro Arg Gly Val Pro Gln Ile Lys Val Thr Phe 465 470 475 480 Asp Ile Asp Ala Asn Gly Ile Leu Thr Val Ser Ala Ala Asp Lys Ser 485 490 495 Thr Gly Lys Thr Glu His Val Thr Ile Thr Asn Asp Lys Gly Arg Leu 500 505 510 Ser Gln Gln Asp Ile Asp Arg Met Val Ala Glu Ala Glu Lys Phe Arg 515 520 525 Glu Asp Asp Glu Lys Lys Lys Arg Cys Val Glu Ser Lys Asn Glu Leu 530 535 540 Glu Asn Tyr Cys Tyr Ser Met Lys Asn Ala Leu Glu Glu Glu Gly Val 545 550 555 560 Lys Ser Lys Leu Ser Ser Ser Glu Leu Ser Glu Ala Gln Lys Leu Leu 565 570 575 Gln Asn Thr Phe Ser Trp Ile Glu Ser Asn Gln Leu Ala Glu Lys Glu 580 585 590 Glu Phe Glu Ala Lys Leu Lys Glu Val Gln Ala Val Cys Thr Pro Leu 595 600 605 Thr Ala Lys Leu Tyr Gln Ala Gly Gly Gly Val Pro Gly Gly Ala Ala 610 615 620 Pro Gly Gly Phe Asn Ala Gly Gly Ala Ala Pro Ser Gly Pro Thr Val 625 630 635 640 Glu Glu Val Asp <210> 56 <211> 395 <212> PRT <213> babesia microti <400> 56 Met Thr Ala Tyr Ile Pro Gly Leu Leu Glu Arg Leu Ser Ala Pro Ile 1 5 10 15 Val Ser Ser Arg Leu Asp Asp Asp Asp Leu Ala Tyr Leu Gly Lys Tyr 20 25 30 Glu Ser Glu Ile Ser Asp Ser Asp Asn Leu Gln Asn Ile Tyr Ser Asn 35 40 45 Asp Thr Ile Val Ala Leu Gly Asp Leu Asp Ala Lys Tyr Lys Gln Gln 50 55 60 Thr Tyr Leu Ser Ser Leu Asn Ser His Ile Val Asp Gln Asp Ala Gln 65 70 75 80 Ile Ala Phe Tyr Pro Val Lys Tyr Thr Asn Lys Ile Ile Arg Asn Asp 85 90 95 Ser Asn Leu Thr Tyr Arg Arg Thr Thr Ser Ser Leu Ser Asn Pro Leu 100 105 110 Val Asn Tyr Ile Gln Lys Ser Gln His Asp Thr Pro Asp Pro Val Asp 115 120 125 Ser Asn Ile Gln Asn Ser Ser Ser Glu Gln Tyr Ala Ile Thr Thr Ala 130 135 140 Ser Ser Gly Ser Asp Lys Ser Lys Arg Leu Ser His Asp Asn Ser Lys 145 150 155 160 Thr Asp His Asp Ile His Asp Lys Ser Gly Val Val Thr Ala Asn Asn 165 170 175 His Ser Thr Asp Arg Phe Gln Asn Ala Gly Asp Leu Val Trp Gln Pro 180 185 190 Gly Phe Thr Arg Gln Leu Gly Thr Lys Gly Arg Arg Val Leu Leu Asp 195 200 205 Leu Ile Arg Lys Val Tyr Arg Gly Asn Pro Glu Tyr Phe Lys Asn Ile 210 215 220 Leu Ala Leu Lys Asn Pro Pro Thr Ser Ile Ser Asn Leu Pro Phe Cys 225 230 235 240 Asn Val Thr Met Leu Trp Glu Leu Ala Asn Asp Phe Gly Val Phe Asp 245 250 255 Gln Ala Ile Gln Ile His Tyr Ala His Gly Lys Pro Gly Tyr Pro Ala 260 265 270 Asn Tyr His Asn Thr Ala Asn Tyr Gly Cys Asn Lys Thr Arg Lys Thr 275 280 285 Asn Ser Gly Lys Ser Lys Lys Asn Lys Phe Tyr Asn Tyr Asp Tyr Glu 290 295 300 Ala Tyr Asp Glu Tyr Tyr Glu Asp Glu Tyr Ile Ser Ser Phe Ser Asn 305 310 315 320 Gly Arg Thr Ser Arg Gly Arg Lys Ile Val Gln Pro Lys Arg Phe Asp 325 330 335 Asp Tyr Asp His Leu Leu Asp Ser Asn Tyr Gln Val Glu Tyr Gly Tyr 340 345 350 Cys Ser Asn Arg His Leu Asn Lys Asp Gly Asn Thr Ile Leu Tyr Tyr 355 360 365 Lys Asn Lys Ser His Asp Tyr Val Asn Leu Gly Glu Leu Lys Gly His 370 375 380 Lys Ile Glu Arg Phe Thr Ser Gln Leu Ile Cys 385 390 395 <210> 57 <211> 404 <212> PRT <213> babesia microti <400> 57 Met Lys Asn Asp Phe Asn Ser Val Glu Leu Pro Gly His Phe Leu Phe 1 5 10 15 Thr Ser Glu Ser Val Asn Glu Gly His Pro Asp Lys Leu Cys Asp Gln 20 25 30 Ile Ser Asp Ser Ile Leu Asp Ala Cys Leu Glu Gln Asp Pro Glu Ser 35 40 45 Lys Val Ala Cys Glu Val Cys Thr Lys Arg Gly Met Val Met Val Phe 50 55 60 Gly Glu Ile Ser Thr Asn Ala Lys Val Asn Tyr Glu Glu Val Val Arg 65 70 75 80 Asn Val Val Lys Asn Val Gly Tyr Asp Ser Glu Asp Lys Gly Ile Asp 85 90 95 Tyr Lys Thr Met Asp Val Ile Ile Asn Leu Asp Gln Gln Ser His Glu 100 105 110 Ile Ala Gln Ala Val His Leu Gly Lys Asp Ala Asp Asn Thr Cys Ala 115 120 125 Gly Asp Gln Gly Ile Met Phe Gly Tyr Ala Thr Asp Glu Thr Pro Glu 130 135 140 Tyr Met Pro Leu Ser His Ser Leu Ala Thr Gly Leu Gly Lys Arg Leu 145 150 155 160 Lys Asp Val Arg Leu Ser Gly Leu Leu Pro Tyr Leu Gly Pro Asp Gly 165 170 175 Lys Thr Gln Ile Thr Val Glu Tyr Ile Lys Glu Gly Tyr Gly Ser Ile 180 185 190 Lys Pro Ile Arg Val His Thr Val Leu Ile Ser Gln Gln His Ser Ala 195 200 205 Asn Val Ser Asn Asp Lys Leu Arg Glu Asp Leu Met Thr His Val Val 210 215 220 Lys Ala Val Ile Pro Pro His Phe Leu Asp Asp Lys Thr Lys Tyr Tyr 225 230 235 240 Leu Asn Pro Ser Gly His Phe Val Val Gly Gly Pro Ser Ser Asp Ala 245 250 255 Gly Leu Thr Gly Arg Lys Val Ile Val Asp Thr Tyr Gly Gly Trp Gly 260 265 270 Ala His Gly Gly Gly Cys Phe Ser Gly Lys Asp Gly Thr Lys Val Asp 275 280 285 Arg Ser Ala Ala Tyr Tyr Ala Arg Lys Val Ala Lys Ser Leu Val Ala 290 295 300 Asn Gly Phe Cys Arg Arg Ala Leu Val Gln Val Ser Tyr Ser Ile Gly 305 310 315 320 Ile Arg Ser Pro Leu Ser Leu His Val Asp Ser Tyr Asn Thr Cys Ile 325 330 335 Glu Gly Phe Thr Asp Leu Asp Leu Glu Gln Ile Ala Val Arg Asn Phe 340 345 350 Asp Phe Ser Val Gly Asn Ile Ile Lys Glu Leu Gln Leu Lys Lys Pro 355 360 365 Ile Tyr Ser Gln Thr Gly Val Tyr Gly His Phe Gly Lys Asp Asn Pro 370 375 380 Glu Tyr Leu Trp Glu Asn Val Lys Asp Leu Ser His Glu Leu Thr His 385 390 395 400 Lys Pro Lys Arg <210> 58 <211> 467 <212> PRT <213> babesia microti <400> 58 Met Asp Tyr Thr Arg Ser Leu Phe Thr Leu Ser Gly Pro Ala Thr Ala 1 5 10 15 Ser Glu Val Glu Lys His Ile Gln Asn Ala Ile Glu Phe Val Lys Arg 20 25 30 Arg Asp Pro Asp Gln Val Gln Phe Ile Gln Ala Phe Thr Glu Val Ala 35 40 45 Asn Gly Leu Ala Pro Val Phe Gln Thr Asp Leu Lys Tyr Leu Glu Ile 50 55 60 Phe Leu Ser Leu Ser Glu Pro Glu Arg Val Ile Thr Phe Lys Val Pro 65 70 75 80 Trp Val Asn Asp Ala Gly Lys Leu Met Ile Asn Arg Gly Phe Arg Val 85 90 95 Gln Phe Asn Ser Thr Leu Gly Pro Tyr Lys Gly Gly Leu Arg Phe His 100 105 110 Pro Ser Val Asn Leu Ser Ile Leu Lys Phe Leu Gly Phe Glu Gln Ile 115 120 125 Phe Lys Asn Ser Leu Thr Thr Leu Ala Met Gly Gly Gly Lys Gly Gly 130 135 140 Ser Asp Phe Asp Pro Lys Gly Lys Ser Asp Asn Glu Val Arg Ser Phe 145 150 155 160 Cys Gln Ser Phe Met Thr Glu Leu Gln Arg His Ile Gly Pro Asp Thr 165 170 175 Asp Val Pro Ala Gly Asp Ile Gly Val Gly Glu Arg Glu Ile Gly Phe 180 185 190 Met Tyr Gly Gln Tyr Lys Arg Leu Ser Asn Ser Ser Thr Gly Thr Leu 195 200 205 Thr Gly Lys Asp Pro Lys Trp Gly Gly Ser Phe Ile Arg Pro Gln Ala 210 215 220 Thr Gly Tyr Gly Leu Val Phe Phe Val Gln Tyr Ile Leu Asn Asp Leu 225 230 235 240 His Asn Gly Asp Ser Phe Lys Gly Lys Arg Val Ala Ile Ser Gly Ser 245 250 255 Gly Asn Val Ala Gln Tyr Ala Ala Asp Lys Val Ile Asp Phe Gly Gly 260 265 270 Ile Pro Ile Thr Phe Ser Asp Ser Ser Gly Tyr Ile Tyr Glu Pro Asn 275 280 285 Gly Phe Thr Lys Glu Met Val Thr Val Leu Met Glu Leu Lys Asn Ile 290 295 300 Gln Arg Ala Arg Val Ser Glu Phe Leu Lys Tyr Ser Asn Thr Ala Lys 305 310 315 320 Phe Phe Pro Asn Lys Lys Ala Trp Asp Val Asp Thr Asn Val Asn Val 325 330 335 Ala Leu Pro Cys Ala Cys Glu Asn Glu Leu Asp Lys Ala Asp Ala Glu 340 345 350 Met Leu Val Lys Lys Gly Cys Ile Ile Val Gly Glu Gly Ala Asn Met 355 360 365 Pro Thr Thr Pro Glu Ala Ile Ser Val Phe Lys Ala Ala Lys Val Thr 370 375 380 Val Cys Pro Gly Lys Ala Ala Asn Ala Gly Gly Val Ala Val Ser Gly 385 390 395 400 Leu Glu Met Ser Gln Asn Ser Gln Arg Glu Lys Trp Thr Ser Glu Lys 405 410 415 Val Leu Glu Lys Leu Gln Asp Ile Met Lys Asn Met Ser Lys Ala Cys 420 425 430 Gln Glu Ala Ala Ala Lys Tyr Asn Val His Gly Asp Ile Ile Ser Gly 435 440 445 Ala Asn Ile Ala Gly Phe Leu Lys Val Ala His Ser Tyr Cys Asp Gln 450 455 460 Gly Cys Val 465 <210> 59 <211> 433 <212> PRT <213> babesia microti <400> 59 Met Ser Tyr Ser Ala Glu Glu Thr Asp Ala Ser Ile Glu Gln Trp Lys 1 5 10 15 Ile Leu Arg Leu Ile Arg Asn Leu Glu Ser Ala Lys Gly Asn Gly Thr 20 25 30 Ser Met Ile Ser Leu Ile Ile Lys Pro Lys Asp Glu Ile Ala Arg Ile 35 40 45 Asn Lys Met Leu Ala Asp Glu Phe Gly Thr Ala Ser Asn Ile Lys Ser 50 55 60 Arg Val Asn Arg Leu Ser Val Leu Ser Ala Ile Thr Ser Thr Gln Gln 65 70 75 80 Lys Leu Lys Leu Tyr Arg Gln Thr Pro Pro Lys Gly Leu Val Val Tyr 85 90 95 Cys Gly Thr Ile Leu Thr Glu Asp Gly Lys Glu Lys Lys Val Ser Leu 100 105 110 Asp Phe Glu Pro Phe Lys Pro Ile Asn Thr Ser Leu Tyr Leu Cys Asp 115 120 125 Asn Lys Phe His Val Glu Ala Leu Lys Glu Leu Leu Glu Ser Asp Glu 130 135 140 Lys Phe Gly Phe Ile Ile Val Asp Gly Asn Gly Val Leu Tyr Gly Thr 145 150 155 160 Leu Gln Gly Asn Thr Lys Glu Val Leu His Ser Phe Thr Val Asp Leu 165 170 175 Pro Lys Lys His Gly Arg Gly Gly Gln Ser Ala Leu Arg Phe Ala Arg 180 185 190 Leu Arg Leu Glu Lys Arg His Asn Tyr Val Arg Lys Val Ala Asp Ile 195 200 205 Ala Val Gln Met Phe Ile Thr Asn Asp Arg Pro Asn Val Ser Gly Leu 210 215 220 Val Leu Ala Gly Ser Ala Asp Phe Lys Asn Asp Leu Met Ser Ser Asp 225 230 235 240 Met Phe Asp Pro Arg Leu Ala Ala Lys Val Val Lys Ile Val Asp Val 245 250 255 Ser Tyr Gly Gly Asp His Gly Phe Asn Gln Ala Ile Glu Leu Ser Ala 260 265 270 Gln Cys Leu Ser Asn Val Lys Phe Ile Gln Glu Lys Lys Ile Ile Ser 275 280 285 Arg Phe Phe Asp Glu Leu Ala His Asp Thr Gly Arg Tyr Val Tyr Gly 290 295 300 Val His Asp Thr Ile Asn Ala Leu Glu Met Gly Ala Val Glu Met Leu 305 310 315 320 Ile Val Tyr Glu Ala Leu Asp Ile Gln Arg Leu Gln Met Arg Asn Pro 325 330 335 Val Thr Gly Glu Glu Ser Val Ile Ile Gln Thr Ser Glu Arg Asp Thr 340 345 350 Glu Ala Met Arg Asp Pro Val Asn Asn Val Asp Leu Glu Leu Val Glu 355 360 365 Ser Ile His Leu Ser Glu Trp Leu Val Asn Asn Tyr Arg Asn Tyr Gly 370 375 380 Ala Thr Leu Glu Phe Ile Thr Asn Lys Ser Gln Glu Gly Ser Gln Phe 385 390 395 400 His Arg Gly Phe Gly Gly Ile Gly Gly Ile Leu Arg Tyr Lys Leu Asp 405 410 415 Met Ser Glu Tyr Asp Leu Pro Val Asn Asp Asn Asp Phe Asp Asp Phe 420 425 430 Ile <210> 60 <211> 1094 <212> PRT <213> babesia microti <400> 60 Met Asp Ser Leu Val Pro Pro Tyr Asn Lys Leu Asn Phe Asp Ile Ser 1 5 10 15 Arg Pro Asp Ile Ser Gly Asn Thr Leu His Tyr Thr Phe Phe Gln Tyr 20 25 30 Pro Asp Ser Ser Ile Ser Lys Leu Arg Asn Val Phe Ala His Asn Pro 35 40 45 Gln Gln Asn Phe Thr Asn Gln Pro Phe Tyr Pro Pro Lys His Asn Asp 50 55 60 Thr Pro His Thr Glu Gln Asn Gly Ser Gln Phe Ile His Ser Asn Ser 65 70 75 80 Asn Thr Ser Asn Asn Leu Glu Ser Asn Asp Val Asp Asn Asn Ala Ser 85 90 95 Ala Ser Ala Cys Asp Lys Arg Ser Phe Pro His Asp Asp Arg Tyr Ser 100 105 110 Ser Ser Asn Tyr Asn Glu Tyr Pro Gly Ile Leu Ser Ser Ile Gln Asp 115 120 125 Ile Ala Asp Leu Phe Asp Leu Asp Asn Tyr His Ile Tyr His Gly Ile 130 135 140 Asp Asn Ile Ser Tyr Leu Thr Tyr Ser Thr Asp Ala Asn Arg Thr Gly 145 150 155 160 Ile Asp Ser Lys Leu Glu Phe Ile Tyr Glu Val Leu Asn Ser Asn Gly 165 170 175 Ser Asn Met Thr Leu Ser Lys Leu Glu Gly Phe Leu Arg Ile Leu Thr 180 185 190 Thr Asp Asp Asn Pro Ile Gly Thr Leu Thr Pro Tyr Gly Ser Leu Met 195 200 205 Ala His Thr Cys Leu Arg Phe Leu Lys Ser Tyr Ile Arg Thr Asp Asn 210 215 220 Lys Gly Asn Ser His Asp Pro Asp Thr Phe Ile Tyr Ser Ile Glu Gly 225 230 235 240 Lys Lys Gly Lys Ser Lys Leu Ser Lys Gln Gly Ile Thr Asn Glu Asn 245 250 255 Glu Thr Thr Thr Val Ser Ser Asp Phe Arg Arg Ile Ala Met Phe Asn 260 265 270 Phe Glu Leu Tyr Ser Lys Gln Leu Met Asp Thr Ile His Ser Gln Asp 275 280 285 Lys Ser Ile Ala Ile Asn Lys Arg Lys Phe Asp Asp Leu Thr Ser Asn 290 295 300 Tyr Thr Lys Ser Glu Ser Val Ser Ile Asp Ser Met Ser Ala Ile Ser 305 310 315 320 Asp Ser Thr Asp Lys Arg Ala Val Ser Ser Gln Thr Leu Lys Ile Ile 325 330 335 Lys Gln Gly Ser Ala Tyr Leu Gln Asp Phe Ile Ser Lys Tyr Arg Ile 340 345 350 Gly Phe Glu Pro His Phe Pro Arg Ile Val Cys Gly Ser Ile Asp Arg 355 360 365 Ser Leu Val Thr Asn Gln Ala Ser Ile Thr Val Pro Ile Asp Lys Ser 370 375 380 Gly Arg Ser Val His Ile Ala Phe Glu Ala Leu Ser Asp Ser Tyr Gly 385 390 395 400 Met Ser Val Trp Pro Glu Leu Asn Gln Leu Pro Asn Ser Leu Gln Leu 405 410 415 Gly Thr Lys Ile Gln Ile Ala Trp His Lys Thr Pro Gly Asn Met Arg 420 425 430 Trp Tyr Ile Gly Thr Ile Val Gln Ser Thr Ala Ser Gln Tyr Ser Val 435 440 445 Gln Val Tyr Leu Gly Lys Asn Glu Tyr Lys Thr Arg Tyr Cys Thr Met 450 455 460 Lys Tyr Phe Val Pro Pro Asn Val Pro Val Val Lys Pro Asp Asn Thr 465 470 475 480 Trp Trp Arg Leu Val Pro Arg Glu Ile Asn Leu Ser Thr Asp Leu Tyr 485 490 495 Val Gly Ser Cys Val Ser Leu Tyr Asp Ile Ile Ser Asn Phe Glu Ser 500 505 510 Ile Asp Cys Val Ile Cys Asn Val Tyr Tyr Ser Asn Asp Asn Ser Pro 515 520 525 Asn Gly Pro Ile Lys Gly Pro Asn Glu Glu Ile Tyr Lys Ser Asp Lys 530 535 540 Ser Ser Ser Gly Phe Lys Ile Gln Leu Asn Cys Ala Cys His Gly Pro 545 550 555 560 Thr Arg Arg Ile Arg Gln Gly Val Leu Thr Thr Gly Val Val Arg Val 565 570 575 His Ile Tyr Cys Met Ser His Lys Ile Asp Lys Ile Ile Pro Ile Asp 580 585 590 Ser Ile Arg Gly Tyr Lys Leu Asn Tyr Asp Leu His Ala His Phe Asp 595 600 605 Gly Gln Pro Asp Tyr Gly Pro Leu Met Gln Ser Thr Thr Trp Thr Trp 610 615 620 Val Ile Pro Arg Leu Val Ile Ala Pro Asp Asn Lys Tyr Asp Asp Glu 625 630 635 640 Lys Tyr Trp Thr Ser Asn Pro Lys Tyr Ser Leu Leu Ile Phe Pro Tyr 645 650 655 His Arg Asn Met Glu Tyr Ile Ile Ser Ala Thr Lys Leu Ile Ala Ile 660 665 670 Leu His Pro Glu Leu Asn Val Thr Ser Leu Tyr Asn Asn Gly Glu Trp 675 680 685 Phe Val Arg Gln Glu Gly Asp Ile Ala Ile Lys Gly Tyr Gly Gly Leu 690 695 700 Arg Pro Ser Gly Leu Ser Phe Ser Lys Ile Pro Leu Leu Asp Arg Leu 705 710 715 720 Phe Gly Cys His Arg Ile Lys Val Phe Tyr Asn Val Pro Ile Asp Val 725 730 735 Asn Lys Lys Val Glu Asp Phe Lys Asn Asp Tyr Thr Ile Ser Arg Cys 740 745 750 Ala Asn Cys Arg Gly Ile Tyr Tyr Thr Asp Ile Ser His Ala Ser Asn 755 760 765 Gly Lys Thr Tyr Ile Ser Ser Asp Val Glu Tyr Arg Lys Lys Ile Gln 770 775 780 Ile Ala Ala Ala Ile Arg Trp Lys Arg Val Arg Glu Ser Ser Asn Thr 785 790 795 800 Ile Leu Asn Cys Tyr Asn Glu Asn Asp Glu Leu Val Tyr Arg Thr Lys 805 810 815 Asn Ser Phe Ser Leu Ser Trp Glu Gln Asp Gly Arg Asn Leu Glu Leu 820 825 830 Ala Tyr Arg Arg Ala His Ala Pro Gly Ile Ser Lys Phe Glu Ser Lys 835 840 845 Arg Leu Asp Ser Leu Met Lys Ser Asn Lys Gln Val Ser Asn Val Pro 850 855 860 Glu Asn Met Cys Thr Glu Gly Leu Leu Glu Lys Phe Asn Glu Ser Met 865 870 875 880 Lys Phe Ser Glu Ser Val Lys Ser Thr Asp Ser Lys Asn Ala Ala Lys 885 890 895 Leu Leu Glu Val Ala Ile Leu Gly Gly Trp Met Asn Asp Ser Thr Lys 900 905 910 Thr Glu Ser Ile Asn Thr Asn Lys Gly Asp Asn Ile Phe Arg Tyr Ile 915 920 925 Asn Lys Ser Ile Gln Ala Lys Ala Ala Gln Asp Ala Leu Asp Phe Leu 930 935 940 Lys Asn Cys Ser Pro Pro Cys Leu Ser Lys Gln Val Gly Lys His Tyr 945 950 955 960 Thr Pro Ile Asn Gly Lys Gln Ser Met Phe Lys Gln Gly Gly Met Ser 965 970 975 Asp Tyr Gln Asp Ser Ile Pro His Leu Asp Ile Gly Asn Pro Met Ile 980 985 990 Ser Asp Tyr Asn Ser Lys Lys Val Lys Leu Gln Ser Val Ser Gly Asp 995 1000 1005 Gln Arg Gly Leu Asn Ile Tyr Glu Asn Pro Cys Ile Ala Thr Val 1010 1015 1020 His Asp Pro Ser Val Asn Tyr Asn Ser Leu Arg Asn Phe Leu Ala 1025 1030 1035 Lys Ala Glu Trp Asp Glu Glu Ile Glu Asp Ala Pro Ser His Gly 1040 1045 1050 Val Leu Asp Phe Thr Ile Lys Ser Glu Glu Pro Val His Asn Glu 1055 1060 1065 Ala Gly Glu Asp Cys Ile Tyr Ala Val Pro Ile Asn Asp Ser Val 1070 1075 1080 Asn Ile Ile Trp Ser Asp Thr Glu Asp Ala Lys 1085 1090 <210> 61 <211> 1024 <212> PRT <213> babesia microti <400> 61 Met Val Glu Arg Leu Ile Ala Arg Ser Leu Ser Ile Asp Ser Ile Glu 1 5 10 15 Thr Gln Ile Leu Arg Phe Phe Ser Gly Asp Ile Gly Leu Gln Thr Val 20 25 30 Leu Leu Glu Phe Gln Lys Gly Pro Arg Ala Phe Val Ile Cys Leu Asp 35 40 45 Ile Ile Asn Lys His Cys Lys Glu Phe Ser Ser Lys Ser Leu Pro Leu 50 55 60 Ile Leu Phe Cys Ser Gln Thr Leu Val Glu Cys Asp His Ile Tyr Ser 65 70 75 80 Leu Cys Arg Leu Val Ser Asp Gly Gln Ala Gln Asp Leu Asp Lys Ser 85 90 95 Asp Ala Thr Lys Leu Asp Thr Glu Arg Glu Glu Thr Ile Glu Lys Leu 100 105 110 Glu Arg Val Ile Asn Leu Leu Glu Gln Leu Asn Lys Val Asn Pro Gln 115 120 125 Ile Phe Pro Ser Leu Arg Phe Leu Leu Cys Ala Trp Leu Arg Leu Lys 130 135 140 Leu Phe Asp Asn Trp Ser Lys Gly Ile Thr Phe Glu Ile Ile Gln Phe 145 150 155 160 Val Gly Thr Phe Gln Ser Asn Arg Gln Phe Gln Ile Glu Leu Leu Ala 165 170 175 Ile Leu Ala Gln Glu Ile Cys Asn Asp Lys Phe Ile Leu Ser Ile Ala 180 185 190 Arg Arg Asn Glu Leu Ala Lys Asn Cys Ile Ser Gln Ala Pro Met Val 195 200 205 Phe Lys Phe Leu Gly Val Lys Asp Ser Ser Ile Gly Ser Val Tyr Ser 210 215 220 Asp Trp Ile Gln Leu His Val Lys Tyr Leu Asp Ser Ile Val Asp Glu 225 230 235 240 Glu Gln Cys Glu Leu Pro Ser Asp Val Asp Leu Met Val Lys Leu Ser 245 250 255 Leu Ser Thr Leu Ile Ser Leu Asn Leu Ile Asp Lys Leu Phe Glu Gln 260 265 270 Ser Pro Leu Pro Ile His Thr Ile Thr Asn Leu Ile Val Leu Cys Pro 275 280 285 Leu Asp Asn His Thr Ala Leu Gln Asp Asp Cys Asp Met Ile Asn Pro 290 295 300 Leu Val Asn Glu Ile Leu Thr Leu Ile Ile Cys Asn Leu Ser Lys Leu 305 310 315 320 Tyr Lys Ile Gln Ser Pro Leu Phe Lys Thr Thr Ser Pro Ile Leu Leu 325 330 335 Ser Leu Ser Tyr Glu Gln Leu Pro Tyr Leu Ile Glu His Gln Phe Ser 340 345 350 Glu Asp Ile Asp Asn Ile Leu Asp Gly Thr Ile Arg Ile Leu Ser Asn 355 360 365 Gly Asp Tyr Pro Thr Arg Asp Val Met Val Asn Phe Trp Ile Asn Leu 370 375 380 Lys Arg Asn Ile Asn Thr Gln Asn Gly Trp Glu Lys Leu Ala Asp Tyr 385 390 395 400 Leu Gln Lys Ile Val Ile Val Phe Tyr Glu Met Pro Leu Tyr Glu Thr 405 410 415 Glu Lys Tyr Asp Phe Ala Glu Leu Cys Ser Phe Arg Glu Ser Ala Ser 420 425 430 Met Leu Leu Phe Glu Ile Ala Asp Ala Ile Gly His Gln Phe Ile Phe 435 440 445 Asp Ile Val Glu Cys Arg Leu Gln Val Leu Val Glu Thr Ile Asn Leu 450 455 460 Lys Glu Gln Ile Thr Val Ser Phe Ser Glu Ile Glu Ser Ile Phe Phe 465 470 475 480 Ile Leu Ser Ala Ile Ser Ser Asn Ala Glu Met Gly Lys Asp Thr Cys 485 490 495 Ile Pro Thr Ala Leu Ala Leu Leu Asn Lys Leu Lys Tyr Pro Thr Gln 500 505 510 Gly Ser Leu Ser Leu Leu Leu Ser Ile Ser Ile Gly Arg Leu Ile Leu 515 520 525 Trp Thr Ala Glu Tyr Ser Gly Lys Lys Thr Asp Leu Phe Asn Cys Leu 530 535 540 Phe Met Leu Ile Ile Gly Thr Leu Leu Pro Ser Ile Leu Arg Ile Lys 545 550 555 560 Asn Asn Ser Ala Ser Lys Gly Met Tyr Tyr Tyr Leu Leu Gly Glu Asn 565 570 575 Ile Leu Ile Asp Ala Met Leu Ala Leu Ser Arg Thr Ser Arg Lys Ile 580 585 590 Val Ser Glu Asp Thr Gln Glu Val Lys Lys Tyr Leu Ile Ile Cys Ile Tyr 595 600 605 Gln Ile Ile Lys Asn Val Gln Phe Ser Ile Glu Asn Arg Ile Lys Ala 610 615 620 Val Asn Ala Ala Gly Ala Ile Ile Ser Tyr Met Pro Ile Ala Glu Met 625 630 635 640 Lys Thr Leu Phe Ser Asp Leu Ile Glu Asn Leu Ser Asn Asn Ile Lys 645 650 655 Ser Val Ser Asn Pro Thr Asp Tyr Ile Gln Leu Tyr Leu Met Ala Met 660 665 670 Gln Ser Val Cys Pro Ile Pro Asp Cys Ile Glu Ser Glu Val Ala Ile 675 680 685 Leu Lys Ile Val Glu Lys His Val Ser Val Met Glu Leu Leu Phe Thr 690 695 700 Ser Ser Asn Glu Asp Ile Ile Glu Arg Leu Ser Gln Val Leu Val Val 705 710 715 720 Val Asn Arg Ile Ser Arg Asn His Ser Glu Ala Ser Pro Leu Phe Leu 725 730 735 Trp Thr Leu Lys Leu Leu Ser Val Ser Phe Arg Cys Ser His Pro Ser 740 745 750 His Pro Tyr Ser Ala Leu Arg Ser Ile Leu Ile Asn Val Asn Asp Cys 755 760 765 Ser Val Glu Asn Trp Ala Ser Ile Ser Asn Ser Leu Leu Pro Ser Leu 770 775 780 Ala Met Leu Lys Asp Ser Ile Val Ser Cys Cys Val Gly Asp Lys Asp 785 790 795 800 Arg Asn Leu Leu Gln Gln Gln Met Ser Asp Leu Thr Met Asp Phe Asn 805 810 815 Thr Ser Gln Leu Leu Ser Ala Pro Asp Ser Val Gly Leu Cys Val Asp 820 825 830 Cys Leu Asn Val Ala Leu Asn Arg His Glu Ile Ala Asn Phe Leu Leu 835 840 845 Asp Lys Ser Lys Phe Ile Ile Phe Leu Glu Ser Leu Leu Ile Ile Leu 850 855 860 Pro Tyr Ile Val His Pro Lys Val Leu His Ala Cys Met Ile Leu Ile 865 870 875 880 Lys Leu Val Ala Ser Ile Asp Met Asn Glu Ala Ser Gly Asn Asp Tyr 885 890 895 Ser Asp Ser Ala Val Ile Gly Thr Ser Val Tyr Ala Lys Lys Ile Arg 900 905 910 Leu Leu Asn Ile Ile Ser Gln Arg Cys Asn Glu Ser Ser Asp Glu Ile 915 920 925 His Thr Ile Thr Phe Lys Ile Val Thr Ala Ile Leu Ser Thr Val Ile 930 935 940 Ser Gly Thr Cys Gly Val Glu Thr Trp Ile Asp Val Ala Ala Glu Thr 945 950 955 960 Ile Leu Ala Leu Met Cys Asp Gly Lys Thr Ala Asp Glu Ala Lys Asn 965 970 975 Ala Ile Asp Ser Phe Phe Glu Met Ile Ser Glu Pro Ser Ile Asn Val 980 985 990 Thr Ile Lys Asn Asp Tyr Cys Asn Lys Leu Lys Val Pro Asn Thr Leu 995 1000 1005 Phe Gln Ala Leu Leu Gln Leu Glu Gly Trp Lys Leu Trp Lys Lys 1010 1015 1020 Cys <210> 62 <211> 438 <212> PRT <213> babesia microti <400> 62 Met Arg Gly Met Phe Ser Asn Lys Trp Met Ser Phe Val Cys Phe Ser 1 5 10 15 Ile Leu Phe Val Ala Leu Lys Ser Asp Leu Glu Tyr Val Ser Ala Leu 20 25 30 Lys Leu Leu Arg Ala Pro Pro Gln Thr Ser Leu Phe Leu Glu Lys Leu 35 40 45 Ile Asp Asp Gly Ser Asp Ile Pro Lys Asp Pro Ile Asp Thr Asp Lys 50 55 60 Glu Glu Ser Gln Ser Ser Leu Phe Lys Phe Asn Leu Asn Leu Phe Asn 65 70 75 80 Lys Lys Ser Ile Trp Glu Ala Asp Glu Lys Phe Val Ile Thr Leu Ala 85 90 95 Lys Ser Arg Leu Asn Val Ile Leu Ala Gln Lys Leu Asp Lys Phe Leu 100 105 110 Ala Lys Thr Cys Lys Ile Tyr Thr Val Asp Ser Glu His Ser Ala Cys 115 120 125 Contains Asn Asp Contains Lys Contains Tyr Contains Gln Lys Cys Contains Glu Ser Asn Asp 130 135 140 Leu Asn Ser Cys Tyr Val Ile Pro Ile Gln Pro Ile Ala Lys Leu Pro 145 150 155 160 Thr Ser Arg Leu Tyr Gly Leu Val Pro His Val Leu Asn Phe Ser Ile 165 170 175 Leu Ile Phe Thr Asn Leu Arg Ser Asn Leu Asp Arg Tyr Tyr Ile Asp 180 185 190 Gly Ser Lys Asp Trp Phe Ser His Ile Phe Met Arg Leu Lys Arg Phe 195 200 205 Phe Gly Ile Arg Asn Lys His Ser Tyr Phe Ser Asp Asn Arg Leu Met 210 215 220 Asn Lys Ile Phe Ser Arg Thr Ser Thr Thr Phe Gly Pro Asp Arg Ser 225 230 235 240 Asp Ser Leu Leu Ser Asn Tyr Ile Lys Phe Gly Ala Ile Glu Tyr Ala 245 250 255 You Are The One Thr Arg Will Be The One You Will Be 260 265 270 Phe Ala His Ile Lys Phe Val Arg Lys Arg Leu Tyr Lys Phe Tyr Thr 275 280 285 Asn Lys Trp Lys Ser Ile Glu Gly Leu Val Thr Arg Gly His Leu Lys 290 295 300 Pro Val Asp Leu Ser Asn Asn Pro Ile Ser Asp Asn Ile Phe Lys Tyr 305 310 315 320 Phe Gly Lys Phe Ser Asn Asn Thr Asn Leu Ser Asn Ala Ile Ala Gly 325 330 335 Ala Phe Leu Asp His Tyr Lys Ser Leu Phe Ser Asn Ser Thr Asp Val 340 345 350 Asn Gly Glu Gly Ser Ser Gly Glu Gly Pro Ser Gly Glu Gly Phe Asn 355 360 365 Gly Glu Gly Ser Ser Gly Glu Gly Pro Ser Gly Glu Gly Phe Asn Gly 370 375 380 Glu Gly Phe Asp Gly Glu Gly Pro Ser Gly Glu Gly Pro Ser Gly Glu 385 390 395 400 Gly Phe Asn Gly Glu Gly Phe Asn Gly Glu Gly Leu Asn Gly Glu Gly 405 410 415 Pro Ser Gly Glu Gly Pro Ser Gly Glu Gly Leu Asn Glu Trp Asn Gly 420 425 430 Leu Met Asn Gly Thr Ala 435

Claims

1. 1. A method for detecting a Babesia infection in a subject, the method comprising: detecting whether one or more secretor antigens selected from SEQ ID NOs: 1-62 are present in a biological sample obtained from the subject; detecting the presence of one or more of said antigens in a biological sample indicates that the subject has a Babesia infection.

2. 10. The method of claim 1, wherein the Babesia infection comprises Babesia microti or Babesia duncani.

3. The biological sample comprises: a blood sample, a red blood cell sample, a white blood cell sample, a plasma sample, a urine sample, a saliva sample, and / or a combination of one or more thereof The method of claim 1, comprising one or more species selected from the group consisting of:

4. The method of claim 1, wherein the one or more antigens further include BmGPI12.

5. The method of claim 1, wherein the subject is a human.

6. 10. The method of claim 1, wherein the subject is a mammal known to carry the Babesia parasite.

7. The one or more antigens are selected from the following: Western blot, immunofluorescence assay, IEM, ELISA, PCR-based immunoassay, and immunoprecipitation 2. The method of claim 1, wherein the antibody is detected by one or more antibody-based techniques selected from the group consisting of:

8. assay platform, and Immunological agents having specificity for one or more Babesia antigens selected from SEQ ID NOs: 1-62 10. A diagnostic tool for identifying or diagnosing babesiosis infection, comprising:

9. 9. The diagnostic tool of claim 8, wherein the babesiosis infection comprises a Babesia microti infection or a Babesia duncani infection.

10. The assay platform includes: Enzyme-based assays, radioimmunoassays, PCR-based immunoassays, fluorogenic immunoassays, chemiluminescence-based assays, immunoblotting assays, and combinations thereof The diagnostic tool of claim 8, comprising one or more species selected from the group consisting of:

11. 9. The diagnostic tool of claim 8, wherein the immunological agent comprises one or more of an antibody or an antibody fragment.

12. 1. A method of treating, ameliorating, and / or preventing a Babesia infection in a subject in need thereof, comprising the steps of: obtaining a first sample from a subject at a first time point; Assaying the sample with the diagnostic tool of claim 8 to detect the presence or absence of infection compared to a comparative reference control; administering one or more therapeutic agents to the subject; obtaining a second sample from the subject at a second timepoint, the second timepoint comprising one or more timepoints after the first timepoint; and Assaying a second sample obtained from the subject at a second time point using the diagnostic tool of claim 8 to detect the presence or absence of infection compared to a comparative standard control.

13. 13. The method of claim 12, wherein the sample comprises a blood sample.

14. 13. The method of claim 12, wherein the infection comprises a Babesia microti infection or a Babesia dunkani infection.

15. 13. The method of claim 12, wherein the first time point is before administering the therapeutic agent.

16. 14. The method of claim 13, wherein the second time point is after administering the therapeutic agent.

17. 1. A method of treating, ameliorating, and / or preventing a Babesia infection in a subject, comprising: detecting the presence of one or more peptides selected from SEQ ID NOs: 1-62 in a biological sample obtained from the subject; and administering at least one antiprotozoal treatment to the subject.

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