Method for prevention or treatment of coronavirus infection

Abstract

The invention is in the field of medical treatment and relates to a method for treating coronavirus infection. In particular, the present invention relates to methods for prophylactic and / or therapeutic treatment of coronavirus infection by means of the mucosal administration of antibodies against coronavirus.

Description

[0001] METHOD FOR PREVENION OR TREATMENT OF CORONAVIRUS INFECTION FIELD OF THE INVENTION The invention is in the field of medical treatment and relates to a method for treating coronavirus infections in animals and humans, including Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). In particular, the present invention relates to methods for prophylactic and / or therapeutic treatment of SARS-CoV-2 by means of mucosal administration, especially intranasal and / or oral inhalation of antibodies against β-coronavirus, in particular SARS-CoV-2. BACKGROUND OF THE INVENTION The SARS-CoV-2 virus causes the disease COVID-19 in humans and is widespread having a significant impact on human society. We should expect the SARS-CoV-2 virus and its variants of concern to continue to cause frequent infections, as well as severe disease and death. As of January 2023, the ongoing COVID-19 pandemic caused by SARS-CoV-2, has resulted in more than 6.7 million worldwide deaths since 2019. In recent years, outbreaks of other coronaviruses have caused severe illness and deaths. As scientists develop therapeutic antibodies and vaccines against SARS-CoV-2, the danger remains of future novel variants of SARS-CoV-2 and novel coronaviruses emerging. These novel coronaviruses can lead to morbidity, mortality, and could cause pandemics. It remains vitally important to identify broadly protective therapies that can combat current and emerging coronaviruses in the future. In addition to SARS-CoV-2, six other coronaviruses are known to cause disease in humans: the betacoronaviruses HCoV-OC43 (human coronavirus OC43), HCoV-HKU1 (human coronavirus HKU1), SARS-CoV (severe acute respiratory syndrome coronavirus) and MERS-CoV (Middle East respiratory syndrome coronavirus) and the alphacoronaviruses. Spillover events, where humans get infected with coronaviruses that circulate in animal reservoirs, are common. Recently, three betacoronaviruses crossed from animals to humans, including SARS-CoV-2 causing serious outbreaks. Furthermore, two coronaviruses previously linked only to animal infection were recently detected in humans who presented with flu-like symptoms. Coronaviruses derive their name from their crown-like appearance. Coronaviruses are a large group of viruses that have spike proteins on their surface, resembling crown-like thorns. The antibodies elicited by natural infection or by COVID-19 vaccines used for mass immunization between 2020-2023 primarily target the variable receptor binding domain (RBD) present on these spike proteins. Structure of the spike protein Coronavirus infection is a multistep process that involves enzymatic cleavage and rearrangement of the surface spike protein. The spike protein has an S1 subunit with the receptor-binding domain and an S2 subunit involved in fusion of the viral and cell membranes thereby facilitating cell entry. The viral spike protein of SARS-CoV-2 facilitates viral entry by binding primarily to the angiotensin-converting enzyme 2 (ACE2) receptor on human cells. The SARS-CoV-2 spike contains two cleavage sites: a furin cleavage site at the boundary of the S1 and S2 subunits, and an S2’ site that is highly conserved among different coronaviruses. S1 subunit The SARS-CoV-2 spike protein uses the RBD on the S1 subunit to engage the target cell’s ACE2 receptor. The S1 subunit is more accessible and remains the main target of many neutralizing antibodies. The S1 subunit, however, is more genetically variable than the S2 subunit; especially when subjected to the selective pressure from antibodies. This propensity towards genetic variability can lead to viral variants with the predominant changes occurring on the S1 subunit. Changes in the receptor-binding domain in SARS-CoV-2 variants of concern have resulted in frequent reinfections, as protection by the antibodies elicited by previous infection and / or vaccines dramatically reduced. S2 subunit The viral spike components essential to infection also involve the structurally complex S2 subunit. The S2 subunit contains dynamic elements essential for fusion with the host cell. Once the receptor has bound, the S1 subunit is discarded and the membrane enzyme transmembrane serine protease 2 (TMPRSS2) or endosomal cathepsins cleave the S2 site. This cleaving leads to insertion of the fusion peptide into the cell membrane culminating in viral fusion. These S2 subunit elements are less disposed towards genetic variability than the RBD, which so far has been capable of retaining or even increasing binding capabilities to ACE2 despite a variety of mutations. The S2 domain sites yield poorly accessible targets for novel therapeutics to protect against a wider range of coronaviruses. The fusion peptide The fusion peptide is a domain located on the Spike protein of coronaviruses that is involved in membrane fusion between the viral envelope and host cell upon infection. Some parts of the S2 subunit are called cryptic epitopes, which are hidden antigenic sites because of their presence on the surface that become buried and are only accessible after conformational changes. Unlike the stem helix, which is always available for binding, antigenic sites such as the fusion peptide are considered cryptic, meaning they are hidden until receptor (ACE2) engagement. The latest Omicron variants may protect cryptic epitopes by closely packing the RBDs in the down state and possibly stabilizing the S2- closed state. Treatments and prevention Limited options for the viral treatment of SARS-CoV-2 exist in the form of small molecule or antibody antiviral drugs. For prevention of SARS-CoV-2 infection, few interventions exist. Most are non-pharmaceutical interventions such as social distancing and mask wearing. These methods are non-specific, and efficacy largely depends on compliance. Thus, there is a need for different treatments, especially treatments that simultaneously target the multitude of SARS-CoV-2 variants of concern such as, for example, broad- neutralizing antibodies (bnAbs). Although treatment of SARS-CoV-2 infection with one, two or more antibodies is a possibility, a treatment comprising a single antibody or combination of antibodies would be considerably more cost-efficient. The currently dominant SARS-CoV-2 Omicron subvariant BA.5 is resistant to most monoclonal antibody therapeutics. Betacoronaviruses, including SARS-CoV-2, and alphacoronaviruses also infect a range of species know to have frequent human contact, thus increasing the risk of zoonotic transfer and new outbreaks with SARS-CoV-2 variants or viruses that previously have not infected humans and for which no therapies exist. There is therefore an urgent need to develop therapeutic mAbs that broadly target β- coronaviruses, as well as new SARS-CoV-2 variants of concern that are not neutralized by antibodies elicited by immunization and / or natural infection. It remains vitally important to identify broadly protective therapies that can combat novel coronaviruses. We have surprisingly developed a novel array of broadly protective antibodies which are disclosed herein. SUMMARY OF THE INVENTION The inventors have discovered that an antibody having complementarity-determining regions (CDR) as disclosed herein can advantageously be used in the treatment of a coronavirus infection, especially in the prophylactic treatment of coronavirus infection. The inventors have surprisingly established when treating a coronavirus infection, mucosal administration of an antibody having CDRs as disclosed herein is a more potent prophylactic route of administration method compared with intraperitoneal administration. The inventors have surprisingly established when treating a coronavirus infection, intranasal administration of an antibody having CDRs as disclosed herein is a more potent prophylactic route of administration method compared with intraperitoneal administration. Significantly, the mucosal administration method of treatment of the present invention is effective against SARS-Cov-2 and variants of concern and does not require the use of additional antibodies. A mucosal administration treatment method of the invention is effective even at low dosages and counteracts body weight loss. Complementarity-determining regions (CDRs) Preferably, CDR regions are according to Kabat et al., (1991) as described in Sequences of Proteins of Immunological Interest. In a preferred embodiment, the invention provides an antibody that comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. In a preferred embodiment, the invention provides an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, wherein the antibody is administered to mucosal epithelium. In a preferred embodiment, the invention provides a method for the treatment of a coronavirus infection in an individual, the method comprising administering to an individual in need thereof an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, wherein the antibody is administered to mucosal epithelium. In a preferred embodiment, the invention provides a mucosal composition comprising an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. In a preferred embodiment, the invention provides an antibody for use in a method for treatment of a coronavirus infection in an individual, wherein the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, wherein the antibody is administered to mucosal epithelium. In a preferred embodiment, the invention provides an antibody, or a method or composition comprising the antibody, wherein the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising SEQ ID NO: 013, a heavy chain CDR2 region comprising SEQ ID NO: 170, and a heavy chain CDR3 region comprising SEQ ID NO: 266, a light chain variable domain that comprises a light chain CDR1 region comprising SEQ ID NO: 386, a light chain CDR2 region comprising SEQ ID NO: 439, and a light chain CDR3 region comprising SEQ ID NO: 584. In a preferred embodiment, the invention provides an antibody, or a method or composition comprising the antibody, wherein the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region consisting of SEQ ID NO: 013, a heavy chain CDR2 region consisting of SEQ ID NO: 170, and a heavy chain CDR3 region consisting of SEQ ID NO: 266, a light chain variable domain that comprises a light chain CDR1 region consisting of SEQ ID NO: 386, a light chain CDR2 region consisting of SEQ ID NO: 439, and a light chain CDR3 region consisting of SEQ ID NO: 584. In a preferred embodiment, an antibody is disclosed herein for use in a method for the prophylactic treatment of a coronavirus infection, in an individual, the antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, and wherein between 0.1 mg and 20 mg of the antibody is administered to the mucosa. In a preferred embodiment, an antibody is disclosed herein for use in a method for the prophylactic treatment of a coronavirus infection, in an individual, the antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, and wherein between 0.1 mg and 20 mg of the antibody is administered intranasally. In a preferred embodiment, an antibody is disclosed herein for use in a method for the prophylactic treatment of a coronavirus infection, in an individual, the antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, and wherein between 0.1 mg and 20 mg of the antibody is administered by oral inhalation. In a preferred embodiment, a composition comprising an antibody is disclosed herein, the antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, for use in a method of prevention or treatment of a coronavirus infection, wherein the administration route comprises at least one of pulmonary administration, nasal administration and oropharyngeal administration and wherein the nominal dose of the antibody is between 0.1 mg and 20 mg. Preferably, an antibody as disclosed herein comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315. Preferably, an antibody as disclosed herein comprises a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. Preferably, in a method for treatment of the invention, the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315. Preferably, in a method for treatment of the invention, the antibody comprises a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. In an alternative preferred embodiment, the invention provides an antibody that comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 014 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 171 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 267 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 387 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 440 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 585 to 589, 613 to 618, 634 to 639. Embodiments having > 1 CDRs Preferably, an antibody as disclosed herein comprises a heavy chain variable domain that comprises a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196. Route of administration In a preferred embodiment, the invention provides an antibody as disclosed herein, or a method or composition comprising the antibody as disclosed herein, wherein the antibody is administered by mucosal administration. In a preferred embodiment, the invention provides an antibody as disclosed herein, or a method or composition comprising the antibody as disclosed herein, wherein the antibody is administered by intravenous administration. In a preferred embodiment, the invention provides an antibody as disclosed herein, or a method or composition comprising the antibody as disclosed herein, wherein the antibody is administered by at least one of oral inhalation, nasal administration, ocular administration, vaginal administration, rectal administration and oropharyngeal administration. In a preferred embodiment, the antibody as disclosed herein is administered intranasally. Such an antibody is useful for the treatment of coronavirus infection in an individual. Preferably, the method for treatment of coronavirus infection is a method for prophylactic and / or therapeutic treatment of a coronavirus infection. Preferably, the antibody is provided to an individual infected with coronavirus. Preferably, the antibody is provided to the individual prophylactically. Preferably, the antibody is provided to the individual after infection but prior to onset of symptoms. In a preferred embodiment, the disclosure provides a method of treating coronavirus infection in an individual, said method comprising mucosal administration, preferably administering intranasally and / or by oral inhalation, to an individual in need thereof an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. In a preferred embodiment, the individual is infected with coronavirus or at risk of coronavirus infection. In a preferred embodiment, the disclosure provides an antibody as disclosed herein for use in the manufacture of a medicament for use in the treatment of a coronavirus infection. Clauses The following numbered clauses each represent preferred embodiments of the invention and are part of the description. Clause 1: A method for the treatment of a coronavirus infection in an individual, the method comprising administering to an individual in need thereof an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, wherein the antibody is administered to the mucosa. Clause 2: A mucosal composition comprising an antibody comprising a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. Clause 3: An antibody for use in a method of prevention or treatment of a coronavirus infection in an individual, wherein the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, a heavy chain CDR2 region comprising any one of SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, and a heavy chain CDR3 region comprising any one of SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, a light chain variable domain that comprises a light chain CDR1 region comprising any one of SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, a light chain CDR2 region comprising any one of SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, and a light chain CDR3 region comprising any one of SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639, wherein the antibody is administered to mucosa. Clause 4: A method, composition or antibody according to any preceding Clause, wherein the antibody comprises a heavy chain variable domain that comprises a heavy chain CDR1 region comprising SEQ ID NO: 013, a heavy chain CDR2 region comprising SEQ ID NO: 170, and a heavy chain CDR3 region comprising SEQ ID NO: 266, a light chain variable domain that comprises a light chain CDR1 region comprising SEQ ID NO: 386, a light chain CDR2 region comprising SEQ ID NO: 439, and a light chain CDR3 region comprising SEQ ID NO: 584. Clause 5: A method, composition or antibody according to any preceding Clause, wherein the method for treatment of coronavirus virus infection is a method for prophylactic and / or therapeutic treatment of a coronavirus, preferably wherein the method for treatment is for the prophylactic treatment of a SARS-COV-2 infection. Clause 6: A method, composition or antibody according to any preceding Clause, wherein the antibody comprises a heavy chain variable domain having the sequence of SEQ ID NO: 640 having at most 15, preferably 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acid insertions, deletions, substitutions which are not in the heavy chain CDRs. Clause 7: A method, composition or antibody according to any preceding Clause, wherein the antibody comprises a light chain variable domain having the sequence of SEQ ID NO: 641 having at most 15, preferably 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acid insertions, deletions, substitutions which are not in the light chain CDRs. Clause 8: A method, composition or antibody according to any preceding Clause, wherein the antibody is an IgG antibody, preferably an IgG1 antibody. Clause 9: A method, composition or antibody according to any preceding Clause, wherein the antibody is provided to the individual prophylactically. Clause 10: A method, composition or antibody according to any preceding Clause, wherein the administration route comprises at least one of oral inhalation, nasal administration, ocular administration and oropharyngeal administration. Clause 11: A method, composition or antibody according to any preceding Clause, wherein the antibody is administered at least once or at least twice monthly. Clause 12: A method, composition or antibody according to any preceding Clause, wherein the antibody is administered to the individual at a dosage of between 0.01 mg and 20 mg. Clause 13: A composition according to any preceding Clause, comprising an antibody in a single dose unit of between 0.01 mg and 20 mg, preferably between 0.1 mg and 15 mg or preferably 0.5 mg and 10 mg, wherein the antibody is as defined in any one of claims 1 to 12. Clause 14: A composition according to any preceding Clause, wherein the composition is self- administered. Clause 15: A medicament delivery device comprising a composition according to any preceding Clause. Dosing Preferably, between 0.01 mg and 20 mg of the antibody is administered to an individual, more preferably between 0.1 mg and 20 mg of the antibody is administered to an individual. The flat dose, or nominal dose, of the antibody is preferably between 0.01 mg and 17 mg, preferably between 0.011 mg and 16 mg, preferably between 0.012 mg and 15 mg, preferably between 0.013 mg and 14 mg, preferably between 0.014 mg and 13 mg, preferably between 0.015 mg and 12 mg, preferably between 0.016 mg and 11 mg, preferably between 0.017 mg and 10 mg, preferably between 0.018 mg and 9 mg, preferably between 0.020 mg and 8 mg, preferably between 0.023 mg and 7 mg, preferably between 0.025 mg and 6 mg, preferably between 0.030 mg and 5 mg, preferably between 0.040 mg and 4 mg, preferably between 0.050 mg and 3 mg, preferably between 0.075 mg and 2 mg, or preferably between 0.10 mg and 1 mg. The flat dose, or nominal dose, of the antibody is preferably between 0.010 mg and 5.0 mg, preferably between 0.020 mg and 4.5 mg, preferably between 0.030 mg and 4.0 mg, preferably between 0.040 mg and 3.5 mg, preferably between 0.050 mg and 3.0 mg, preferably between 0.060 mg and 2.5 mg, preferably between 0.070 mg and 2.0 mg, preferably between 0.080 mg and 1.5 mg, preferably between 0.090 mg and 1.0 mg, or preferably between 0.100 mg and 0.5 mg. The flat dose, or nominal dose, of the antibody is preferably between 0.010 mg and 15.0 mg, preferably between 0.020 mg and 14.5 mg, preferably between 0.030 mg and 4.0 mg, preferably between 0.040 mg and 13.5 mg, preferably between 0.050 mg and 13.0 mg, preferably between 0.060 mg and 12.5 mg, preferably between 0.070 mg and 12.0 mg, preferably between 0.080 mg and 11.5 mg, preferably between 0.090 mg and 11.0 mg, or preferably between 0.100 mg and 10.5 mg. The flat dose, or nominal dose, of the antibody to be delivered to a human subject is preferably between 0.1 µg and 10 µg, preferably between 0.2 µg and 9 µg, preferably between 0.3 µg and 8 µg, preferably between 0.4 µg and 7 µg, preferably between 0.5 µg and 6 µg, preferably between 0.6 µg and 5 µg, preferably between 0.7 µg and 4 µg, preferably between 0.8 µg and 3 µg, preferably between 0.9 µg and 2 µg or preferably around 1 µg. The flat dose, or nominal dose, of the antibody to be delivered to a human subject is preferably between 1 mg and 11 mg, preferably between 2 mg and 12 mg, preferably between 3 mg and 13 mg, preferably between 4 mg and 14 mg, preferably between 5 mg and 15 mg, preferably between 6 mg and 16 mg, preferably between 7 mg and 17 mg, preferably between 8 mg and 18 mg, preferably between 9 mg and 19 mg, or preferably between 10 mg and 20 mg. The flat dose, or nominal dose, of the antibody to be delivered to a human subject is preferably between 1 mg and 20 mg, preferably between 2 mg and 19 mg, preferably between 3 mg and 18 mg, preferably between 4 mg and 17 mg, preferably between 5 mg and 16 mg, preferably between 6 mg and 15 mg, preferably between 7 mg and 14 mg, preferably between 8 mg and 13 mg, preferably between 9 mg and 12 mg, or preferably between 10 mg and 11 mg. The flat dose, or nominal dose, of the antibody to be delivered to a human subject is preferably between 11 mg and 20 mg, preferably between 10 mg and 19 mg, preferably between 9 mg and 18 mg, preferably between 8 mg and 17 mg, preferably between 7 mg and 16 mg, preferably between 6 mg and 15 mg, preferably between 5 mg and 14 mg, preferably between 4 mg and 13 mg, preferably between 3 mg and 12 mg, preferably between 2 mg and 11 mg, or preferably between 1 mg and 10 mg. In a preferred embodiment, the disclosure further provides a composition formulated for mucosal administration comprising an antibody as disclosed herein in a single dose unit of between 0.1 mg and 20 mg, preferably between 5 mg and 15 mg or preferably 7.5 mg and 12.5 mg. In a preferred embodiment, the disclosure further provides a composition formulated for intranasal administration comprising an antibody as disclosed herein in a single dose unit of between 0.1 mg and 20 mg, preferably between 5 mg and 15 mg or preferably 7.5 mg and 12.5 mg. In a preferred embodiment, the disclosure further provides a composition formulated for oral inhalation comprising an antibody as disclosed herein in a single dose unit of between 0.1 mg and 20 mg, preferably between 5 mg and 15 mg or preferably 7.5 mg and 12.5 mg. Timing and intervals Preferably, the antibody is administered at least once or at least twice per month. Preferably, the antibody is administered at least once or at least twice per week. The weekly flat dose, or nominal dose, of the antibody is between 0.010 mg and 17 mg, preferably between 0.011 mg and 16 mg, preferably between 0.012 mg and 15 mg, preferably between 0.013 mg and 14 mg, preferably between 0.014 mg and 13 mg, preferably between 0.015 mg and 12 mg, preferably between 0.016 mg and 11 mg, preferably between 0.017 mg and 10 mg, preferably between 0.018 mg and 9 mg, preferably between 0.020 mg and 8 mg, preferably between 0.023 mg and 7 mg, preferably between 0.025 mg and 6 mg, preferably between 0.030 mg and 5 mg, preferably between 0.040 mg and 4 mg, preferably between 0.050 mg and 3 mg, preferably between 0.075 mg and 2 mg, or preferably between 0.10 mg and 1 mg. The weekly flat dose, or nominal dose, of the antibody is between 0.010 mg and 5.0 mg, preferably between 0.020 mg and 4.5 mg, preferably between 0.030 mg and 4.0 mg, preferably between 0.040 mg and 3.5 mg, preferably between 0.050 mg and 3.0 mg, preferably between 0.060 mg and 2.5 mg, preferably between 0.070 mg and 2.0 mg, preferably between 0.080 mg and 1.5 mg, preferably between 0.090 mg and 1.0 mg, or preferably between 0.100 mg and 0.5 mg. Preferably, the antibody is administered at least once or at least twice per day. Preferably, the antibody is administered daily. Preferably, the antibody is administered twice daily. Preferably, the daily flat dose, or nominal dose, is between 0.001 mg and 17 mg, preferably between 0.011 mg and 16 mg, preferably between 0.012 mg and 15 mg, preferably between 0.013 mg and 14 mg, preferably between 0.014 mg and 13 mg, preferably between 0.015 mg and 12 mg, preferably between 0.016 mg and 11 mg, preferably between 0.017 mg and 10 mg, preferably between 0.018 mg and 9 mg, preferably between 0.020 mg and 8 mg, preferably between 0.023 mg and 7 mg, preferably between 0.025 mg and 6 mg, preferably between 0.030 mg and 5 mg, preferably between 0.040 mg and 4 mg, preferably between 0.050 mg and 3 mg, preferably between 0.075 mg and 2 mg, or preferably between 0.10 mg and 1 mg. Framework regions Preferably, the antibody comprises a heavy chain variable domain having the sequence of SEQ ID NO: 640 and / or a light chain variable domain having the sequence of SEQ ID NO: 641. Preferably, the heavy chain variable domain of said antibody further comprises a heavy chain framework region FR1 of SEQ ID NO: 642, a heavy chain framework region FR2 of SEQ ID NO: 643, a heavy chain framework region FR3 of SEQ ID NO: 644, and / or a heavy chain framework region FR4 of SEQ ID NO: 645. Preferably, said light chain variable domain further comprises a light chain framework region FR1 of SEQ ID NO: 646, a light chain framework region FR2 of SEQ ID NO: 647, a light chain framework region FR3 of SEQ ID NO: 648, and / or a light chain framework region FR4 of SEQ ID NO: 649. Combination compositions In a preferred embodiment, we disclose a composition comprising a First binding fragment as disclosed herein and a Second binding fragment, wherein the First fragment comprises a sequence comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. More preferably wherein the First fragment comprises a sequence comprising any one or more of SEQ ID NO: 013, 170, 266, 386, 439 or 584. The Second binding fragment comprises a sequence comprising any one of SEQ ID NO.: 650, 651, 652, 653, 654 or SEQ ID NO.: 655. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose a composition comprising a First binding fragment as disclosed herein and a Second binding fragment, wherein the First fragment comprises a sequence comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. More preferably wherein the First fragment comprises any one or more of SEQ ID NO: 013, 170, 266, 386, 439 or 584. The Second binding fragment comprises a sequence comprising any one of SEQ ID NO.: 656, 657, 658, 659, 660 or SEQ ID NO.: 661. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose a composition comprising a First binding fragment as disclosed herein and a Second binding fragment, wherein the First fragment comprises a sequence comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. More preferably wherein the First fragment comprises a sequence comprising any one or more of SEQ ID NO: 013, 170, 266, 386, 439 or 584. The Second binding fragment comprises a sequence comprising any one of SEQ ID NO.: 662, 663, 664, 665, 666 or SEQ ID NO.: 667. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose a composition comprising a First binding fragment as disclosed herein and a Second binding fragment, wherein the First fragment comprises a sequence comprising any one of SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068, 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196, 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315, 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435, 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528, 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. More preferably wherein the First fragment comprises a sequence comprising any one or more of SEQ ID NO: 013, 170, 266, 386, 439 and 584. The Second binding fragment comprises a sequence comprising any one of SEQ ID NO.: 668, 669, 670, 671, 672 or SEQ ID NO.: 673. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. Bispecific antibodies In a preferred embodiment, we disclose a bispecific antibody, wherein the bispecific antibody is capable of binding to the fusion peptide of a coronavirus. In a preferred embodiment, we disclose a bispecific antibody, wherein the bispecific antibody is capable of binding to the fusion peptide of of the spike protein of SARS-CoV-2. In a preferred embodiment, we disclose an anti- coronavirus bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the stem helix of a coronavirus and a second Fab capable of binding to the fusion peptide of a coronavirus. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the stem helix of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS-CoV-2. In a preferred embodiment, we disclose an anti- coronavirus bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the stem helix of a coronavirus and a second Fab capable of binding to the fusion peptide of a coronavirus. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS- CoV-2. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the stem helix of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 650, 651, 652, 653, 654 to 655; alternatively wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 662, 663, 664, 665, 666 or 667; or alternatively wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 668, 669, 670, 671, 672 to 673, and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 386, 439 or 584; or alternatively wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 656, 657, 658, 659, 660 to 661. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS- CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 656, 657, 658, 659, 660 to 661. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of SARS-CoV-2 and a second Fab capable of binding to the stem helix of SARS- CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 650, 651, 652, 653, 654 to 655. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of SARS-CoV-2 and a second Fab also capable of binding to the stem helix of SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 662, 663, 664, 665, 666 to 667. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose an anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of SARS-CoV-2 and a second Fab also capable of binding to the stem helix of SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 668, 669, 670, 671, 672 to 673. Preferably, the fragment is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 013, 170 or 266, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 671, 672, or 673. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 013, 170 or 266, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 653, 654, or 655. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 013, 170 or 266, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 665, 666, or 667. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 668, 669, or 670, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 386, 439 or 584. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 650, 651, or 652, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 386, 439 or 584. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 662, 663 or 664, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 386, 439 or 584. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 013, 170 or 266, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 659, 660, or 661. In a preferred embodiment, we disclose a bispecific antibody comprising a First Fab and a Second Fab, wherein the First Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 656, 657, or 658, and wherein the Second Fab comprises any one or more of sequences shown in preferred SEQ ID Numbers: 386, 439 or 584. The present invention also provides construction, expression, purification methods for a bispecific antibody having a function of binding to the fusion peptide of SARS-CoV-2, and use of the bispecific antibody in the field of medicine and especially in the prevention and / or treatment of SARS-CoV-2 infections. Clauses The following numbered clauses each represent preferred embodiments of the invention and are part of the description. Clause 26: An anti-coronavirus, preferably anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 656, 657, 658, 659, 660 to 661. Clause 27: A bispecific antibody or an antigen binding fragment thereof according to Clause 26, comprising a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 and / or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 656, 657, 658, 659, 660 and / or 661. Clause 28: A bispecific antibody or an antigen binding fragment thereof according to Clauses 26 or 27, comprising a first Fab specifically binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab specifically binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, characterized in that: a.) the first Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and b.) the second Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 656, a Heavy Chain CDR2 region of SEQ ID NO: 657 and a Heavy Chain CDR3 region of SEQ ID NO: 658 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ ID NO: 659, a Light Chain CDR2 region of SEQ ID NO: 660 and a Light Chain CDR3 region of SEQ ID NO: 661. Clause 29: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 28, comprising: a) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and b) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, wherein the constant domains CL and CH1 from the antibody or an antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, are replaced by each other. Clause 30: A bispecific antibody or an antigen binding fragment thereof according to Clause 29, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 656, a Heavy Chain CDR2 region of SEQ ID NO: 657 and a Heavy Chain CDR3 region of SEQ ID NO: 658 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 659, a Light Chain CDR2 region of SEQ ID NO: 660 and a Light Chain CDR3 region of SEQ ID NO: 661. Clause 31: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 28, comprising: a) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, wherein constant domains CL and CH1 from the antibody that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 are replaced by each other. Clause 32: A bispecific antibody or an antigen binding fragment thereof according to Clause 31, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 656, a Heavy Chain CDR2 region of SEQ ID NO: 657 and a Heavy Chain CDR3 region of SEQ ID NO: 658 and the VL domain of the antibody capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 659, a Light Chain CDR2 region of SEQ ID NO: 660 and a Light Chain CDR3 region of SEQ ID NO: 661. Clause 33: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 28, comprising: a) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, wherein domains VL-CL and VH-CH1 from the antibody that specifically binds to the fusion peptide of a coronavirus, preferably SARS-CoV-2, are replaced by each other. Clause 34: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 33, wherein the first Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 640. Clause 35: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 33, wherein the second Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 684. Clause 36: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 33, wherein the first Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 641. Clause 37: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 33, wherein the second Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 685. Clause 38: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 33, wherein the bispecific antibody or an antigen binding fragment thereof is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. Clause 39: A method for the production of a bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38, comprising a) culturing a host cell, comprising an expression vector, comprising a polynucleotide encoding a bispecific antibody or an antibody fragment according to any one of the preceding Clauses under conditions which permit the production of said bispecific antibody or an antigen binding fragment thereof, and b) isolating said bispecific antibody or an antigen binding fragment thereof. Clause 40: A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or a light chain variable region of the bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38, preferably wherein the nucleic acid molecule is an isolated nucleic acid molecule. Clause 41: A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or light chain variable region of the bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38 and Clause 40, wherein the nucleic acid sequence comprises at least anyone of: (i) a first nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.013, or a first nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO.013, (ii) a second nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 170, or a second nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 170, (iii) a third nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 266, or a third nucleic acid sequence encoding the amino acid sequence having at most 1, 2 or 3 amino acids different from SEQ ID NO. 266, (iv) a fourth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 368, or a fourth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3 or 4 amino acids different from SEQ ID NO. 368, (v) a fifth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.439, or a fifth nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO.439, (vi) a sixth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 584, or a sixth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, or 4 amino acids different from SEQ ID NO. 584, (vii) a seventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.656, or a seventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 656, (viii) an eighth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 657, or an eighth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 657, (ix) a nineth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 658, or a nineth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, or 4 amino acids different from SEQ ID NO. 658, (x) a tenth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 659, or a tenth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, or 4 amino acids different from SEQ ID NO. 659, (xi) an eleventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 660, or an eleventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 660, and (xii) a twelfth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 661, or a twelfth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, or 3 amino acids different from SEQ ID NO. 661. Clause 42: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38 for use in a method of treating a coronavirus infection in a subject. Clause 43: A composition comprising the bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38. Clause 44: A composition according to Clause 43 further comprising a second medicament, for simultaneous, separate, or sequential administration. Clause 45: A composition according to Clause 44, wherein the second medicament comprises a second antibody or antigen binding fragment thereof. Clause 46: A composition according to Clause 44, wherein the second medicament comprises a bispecific antibody or bispecific antigen binding fragment thereof. Clause 47: A composition according to Clause 43, wherein the composition further comprises a pharmaceutically acceptable excipient or carrier. Clause 48: A composition according to Clause 43, for use in inhibiting and / or treating a coronavirus infection in a subject, preferably, a SARS-CoV-1 or SARS-CoV-2 infection in a subject, comprising an effective amount of the bispecific antibody or an antigen binding fragment thereof, nucleic acid molecule, or vector, and optionally a pharmaceutically acceptable excipient or carrier. Clause 49: The composition of Clause 43, for use as a medicament. Clause 50: An inhaler device comprising the composition of Clause 43. Clause 51: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38, wherein the bispecific antibody or an antigen binding fragment thereof is bivalent. Clause 52: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 26 to 38, wherein the bispecific antibody or antigen-binding fragment thereof is capable of binding to the fusion peptide of at least one of an α-coronavirus, β-coronavirus, γ- coronavirus, and δ-coronavirus, preferably at least an α-coronavirus and / or a β- coronavirus. Clauses The following numbered clauses each represent preferred embodiments of the invention and are part of the description. Clause 53: An anti-coronavirus, preferably anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 and a second Fab capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: SEQ ID Numbers: 662, 663, 664, 665, 666 to 667. Clause 54: A bispecific antibody or an antigen binding fragment thereof according to Clause 53, comprising a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 and / or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: SEQ ID Numbers: 662, 663, 664, 665, 666 and / or 667. Clause 55: A bispecific antibody or an antigen binding fragment thereof according to Clauses 53 or 54, comprising a first Fab specifically binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab specifically binding to the stem helix of a coronavirus, preferably SARS-CoV-2, characterized in that: a.) the first Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and b.) the second Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ ID NO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO: 667. Clause 56: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 55, comprising: a) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and b) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein constant domains CL and CH1 from the antibody or an antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS- CoV-2, are replaced by each other. Clause 57: A bispecific antibody or an antigen binding fragment thereof according to Clause 56, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO: 667. Clause 58: A bispecific antibody, or an antigen binding fragment thereof according to any of Clauses 53 to 55, comprising: a) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein constant domains CL and CH1 from the antibody that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 are replaced by each other. Clause 59: A bispecific antibody or an antigen binding fragment thereof according to Clause 58, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and the VL domain of the antibody capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO: 667. Clause 60: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 55, comprising: a) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1-CH2- CH3 domains of an antibody, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein domains VL-CL and VH-CH1 from the antibody that specifically binds to the fusion peptide of a coronavirus, preferably SARS-CoV-2, are replaced by each other. Clause 61: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 60, wherein the first Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 640. Clause 62: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 60, wherein the second Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 688. Clause 63: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 60, wherein the first Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 641. Clause 64: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 60, wherein the second Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO: 689. Clause 65: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 60, wherein the bispecific antibody or antigen binding fragment thereof is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv-Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof. Clause 66: A method for the production of a bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 65, comprising a) culturing a host cell, comprising an expression vector, comprising a polynucleotide encoding a bispecific antibody or an antibody fragment according to any one of the preceding Clauses under conditions which permit the production of said bispecific antibody or an antigen binding fragment thereof, and b) isolating said bispecific antibody or an antigen binding fragment thereof. Clause 67: A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or a light chain variable region of the bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 65, preferably wherein the nucleic acid molecule is an isolated nucleic acid molecule. Clause 68: A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or light chain variable region of the bispecific antibody or the antigen binding fragment thereof according to any of Clauses 53 to 65 and Clause 67, wherein the nucleic acid sequence comprises at least anyone of: (i) a first nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.013, or a first nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO.013, (ii) a second nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 170, or a second nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 170, (iii) a third nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 266, or a third nucleic acid sequence encoding the amino acid sequence having at most 1, 2 or 3 amino acids different from SEQ ID NO. 266, (iv)a fourth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 368, or a fourth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3 or 4 amino acids different from SEQ ID NO. 368, (v) a fifth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.439, or a fifth nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO.439, (vi) a sixth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 584, or a sixth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, or 4 amino acids different from SEQ ID NO. 584, (vii) a seventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.662, or a seventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 662, (viii) an eighth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 663, or an eighth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 663, (ix) a nineth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 664, or a nineth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 664, (x) a tenth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 665, or a tenth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, or 3 amino acids different from SEQ ID NO.665, (xi) an eleventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 666, or an eleventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 666, and (xii) a twelfth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 667, or a twelfth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, or 3 amino acids different from SEQ ID NO. 667. Clause 69: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 65 for use in a method of treating a coronavirus infection in a subject. Clause 70: A composition comprising the bispecific antibody and / or an antigen binding fragment thereof according to any of Clauses 53 to 65. Clause 71: A composition according to Clause 70 further comprising a second medicament, for simultaneous, separate, or sequential administration. Clause 72: A composition according to Clause 71, wherein the second medicament comprises a second antibody or antigen binding fragment thereof. Clause 73: A composition according to Clause 71, wherein the second medicament comprises a bispecific antibody or bispecific antigen binding fragment thereof. Clause 74: A composition according to Clause 70, wherein the composition further comprises a pharmaceutically acceptable excipient or carrier. Clause 75: A composition according to Clause 70, for use in inhibiting and / or treating a coronavirus infection in a subject, preferably, a SARS-CoV-1 or SARS-CoV-2 infection in a subject, comprising an effective amount of the bispecific antibody or an antigen binding fragment thereof, nucleic acid molecule, or vector, and optionally a pharmaceutically acceptable excipient or carrier. Clause 76: The composition of Clause 70, for use as a medicament. Clause 77: An inhaler device comprising the composition of Clause 70. Clause 78: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 65, wherein the bispecific antibody or an antigen binding fragment thereof is bivalent. Clause 79: A bispecific antibody or an antigen binding fragment thereof according to any of Clauses 53 to 65, wherein the bispecific antibody or antigen binding fragment thereof is capable of binding to the stem helix and / or the fusion peptide of at least one of an α-coronavirus, β-coronavirus, γ-coronavirus, and δ-coronavirus, preferably at least an α-coronavirus and / or a β-coronavirus. DESCRIPTION OF THE DRAWINGS Figure 1. Survival after lethal challenge – Antibody according to the invention. Kaplan-Meier survival curves of the intraperitoneal prophylactic treatment group. Animals (n=10 per group), treated with a dose titration with the antibody having heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, at day -1. At day 0, animals were infected with 103.5TCID50 of SARS-CoV-2 Delta. A vehicle control group was included (PBS). Lines are nudged relative to the Y-axis to improve visual representation. Figure 2. Survival after lethal challenge – Antibody according to the invention. Kaplan-Meier survival curves of the intranasal prophylactic treatment group. Animals (n=10 per group), treated with a dose titration with the antibody having heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, at day -1. At day 0, animals were infected with 103.5TCID50of SARS-CoV-2 Delta. A vehicle control group was included (PBS). Lines are nudged relative to the Y-axis to improve visual representation. Figure 3. Bodyweight change – Antibody according to the invention. Bodyweight change (%) relative to day 0, for the intraperitoneal prophylactic treatment group. Animals (n=10 per group) were treated with a dose titration of the antibody having heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, at day -1 intranasally. At day 0 animals were infected with 103.5TCID50of SARS-CoV-2 Delta. A vehicle control group was included (PBS). Bars represent the 95% CI. Of the mean. If a mouse died / was euthanized during follow-up of the study, the last observed bodyweight was carried forward. Figure 4. Bodyweight change – Antibody according to the invention. Bodyweight change (%) relative to day 0, for the intranasal prophylactic treatment group. Animals (n=10 per group) were treated with a dose titration of the antibody having heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, at day -1 intranasally. At day 0 animals were infected with 103.5TCID50 of SARS-CoV-2 Delta. A vehicle control group was included (PBS). Bars represent the 95% CI. Of the mean. If a mouse died / was euthanized during follow-up of the study, the last observed bodyweight was carried forward. Figure 5. Survival and bodyweight change for the intranasal administration – Antibodies according to the invention Survival and bodyweight change for the intranasal administration of two parental antibodies and a bispecific antibody according to invention in a pre-exposure efficacy study in K18-hACE2 mice upon lethal SARS-CoV-2 Delta challenge. Animals (n=8 per group) were treated with a dose titration of either the Parental mAb 1 (Figure 5A-5C), Parental mAb 2 (Figure 5D-5F) or bispecific antibody (Figure 5G-5I) at Day -1 intranasally. At day 0 animals were infected with 103.5TCID50of SARS CoV-2 Delta. A vehicle control group (n=10) was included (PBS). Figures 5A, 5D, 5G: Kaplan-Meier survival curves of the treatment groups is shown. Lines are nudged relative to the Y-axis to improve visual representation. Figures 5B, 5E, 5H: Bodyweight change (%) relative to day 0 is shown. Error bars represent the mean with 95% confidence interval (CI). If a mouse died / was euthanized during follow-up of the study, the last observed bodyweight was carried forward. Figure 5C, 5F, 5I: The survival dose response curves using Probit regression. The vehicle control group was included in the modelling at a dose of 0 mg / kg. The 95% pointwise fiducial confidence intervals for the predicted dose are indicated. Asterisk indicates significance compared to vehicle control group. Figure 6. Linear epitope mapping against Spike fusion peptide domain of alpha and beta coronaviruses Linear epitope mapping against Spike fusion peptide domain of alpha and beta coronaviruses. Grey highlighted amino acids were identified as the epitope where the antibody is binding the Spike protein. Target sequences for the 7 tested strains are aligned by Clustal. *may contain multiple smaller parts of the epitope. Epitope footprints and paratope hotspots for the antibody against the fusion peptide domain of SARS-CoV-2. Heavy and light chain CDRs are indicated. DETAILED DESCRIPTION OF THE INVENTION For the purpose of clarity and a concise description, features may be described herein as part of the same or separate embodiments, however, it will be appreciated that the disclosure includes embodiments having combinations of all or some of the features described. References to “method for treatment”, “treatment method”, “antibody for use” and “use of an antibody in the manufacture of a medicament” can be used interchangeably and embodiments disclosed in relation to any one of those aspects also applies in relation to said other aspects. In other words, they all refer to medical treatments involving an antibody as disclosed herein. Prophylactic treatment The term ‘prophylactic treatment’, as used herein, includes reference to a treatment for preventing infection of an individual with a coronavirus, or preventing symptoms after infection with a coronavirus, or preventing severe symptoms after known infection with a coronavirus with or without symptoms, or preventing hospitalization and death after infection with a coronavirus. Prevention of an infection is preferably performed by administration of an antibody as disclosed herein prior to coronavirus exposure i.e. pre-exposure prophylaxis. ‘Prophylactically’ therefore preferably means prior to virus exposure. Nonetheless, it may also involve administration after infection, for example for reducing the replication or spread, or increasing clearance of the virus i.e. post-exposure prophylaxis. Infected individuals may present with no symptoms. Alternatively, infected individuals may present with symptoms. Preferably, post-exposure prophylaxis involves administering an antibody as disclosed herein after coronavirus exposure to prevent symptomatic disease. Preferably, post-exposure prophylaxis involves administering an antibody as disclosed herein after coronavirus exposure to prevent severe disease, in particular hospitalization. In a treatment method of the invention, prophylactic treatment involves administration of antibodies against coronavirus at a point in time when the individual is not infected with coronavirus. Preferably, said antibodies bind to a conserved epitope of the spike protein of a coronavirus virion. In some embodiments, an individual in need thereof is not (yet) infected with coronavirus. Therapeutic treatment The term ‘therapeutic treatment’, as used herein, includes reference to treatment of a viral infection (including coronavirus disease) after viral infection has taken place. A viral infection involves the entry of the body by the virus, and / or the replication of the virus in the body and / or the spreading of the virus to cells, tissues or locations in the body that were previously uninfected. A viral infection may cause one or more disease, but may also be latent, in other words may reside in the body without causing symptoms or disease. Coronavirus The term ‘coronavirus’, as used herein, includes reference to a positive-sense single- stranded RNA virus belonging to the family of Coronaviridae. Preferably, an antibody as disclosed herein is capable of specifically binding to the fusion peptide of a coronavirus, in particular SARS-CoV-2. Preferably, an antibody as disclosed herein is capable of specifically binding to the fusion peptide of SARS-CoV-2 variants of concern. Preferably, the antibody as disclosed herein is capable of neutralizing a coronavirus, in particular SARS-CoV-2. Preferably, an antibody as disclosed herein is capable of neutralizing at least one or more, preferably two or more, preferably three or more, preferably four or more, even more preferably five or more coronavirus subtypes. The phrase “is capable of” as used in, means the ability of an antibody or an antigen- binding fragment thereof as described herein is enough to bind to at least a part of an antigen, such as the stem helix of a coronavirus, in particular SARS-CoV-2 and / or the fusion protein of a coronavirus, in particular SARS-CoV-2. The binding affinity or the binding ability of the antibody and / or the antigen-binding fragment thereof as described herein can be measured using any methods known by a person skilled in the art. The phrase “is capable of” as used here, encompasses but not limited to the phrase “specifically binding” or “specifically bind to”. Coronavirus infection The term ‘coronavirus infection’, as used herein, includes reference to the pathological or non-pathological, preferably pathological, entrance and residence of a coronavirus of any type in a human host. The infecting virus may replicate within the host, its cells or the cells of its microbiome. The infecting virus may or may not cause a disease, for example COVID-19. The infection may or may not be able to be detected by methods for virus infection detection known in the art. The infected individual may or may not be aware of the infection. Typical, but non-exclusive locations of the human body where, for example SARS-CoV-2, may be located in an infected individual, are the respiratory system and / or cells thereof and the cardiovascular system and / or cells thereof. The term ‘coronavirus infection’, as used herein, further includes reference to the entrance and residence of a part of a coronavirus of any type that is able to cause viral replication in a human host. The term ‘coronavirus infection’ encompasses symptoms or disease following the infection, e.g. COVID-19. The term ‘coronavirus infection’ encompasses ‘SARS-CoV-2 infection’. Epitope An “epitope”, as used herein, includes reference to a moiety that is capable of binding to an antibody as disclosed herein with sufficiently high affinity to form a detectable antigen- antibody complex. Individual The term ‘individual’, as used herein, includes reference to a mammal or human that is subject to, or a risk of suffering from viral infection. Infection may take place in any system, tissue or cell belonging to the host, including the host’s microbiome. Coronavirus infection and the disease coronavirus may occur in individuals of all age groups and sexes. Nonetheless, preferably, the individual is a human, in particular an elderly human such as a human that is at least 60, 65, 70, 75, 80, or at least 85 years old, or that has an increased risk of infection because of occupation or living environment. Preferably, the individual is at risk of suffering from severe illness, for example COVID-19, once infected. In preferred embodiments, the individual has an underlying disease such as (i) a respiratory disease such as asthma, COPD, chronic bronchitis and lung emphysema, (ii) cardiovascular disease such as cardiac arrhythmia or individuals that have received cardiac surgery, (iii) diabetes, (iv) renal failure and / or (v) a disease affecting the immune system, for instance immunocompromised individuals, or higher risk of viral infection because of occupation. The phrase ‘an individual’, as used herein, includes reference to a mammal such as a but not limited to a human that benefits from a specified therapy, for example, the phrase ‘an individual’ may encompass Non-human primates (NHP). Preferably, the individual is a mammal, more preferably a human. Administering and Administration The terms ‘administering’ and ‘administration’, as used herein, include reference to the provision of one or more drug and optionally one or more adjuvant with the aim to treat, cure, reduce, or prevent a disease or its symptoms in an individual, or to promote the individual’s well-being. Preferred methods of administration of the antibody as disclosed herein include mucosal administration, preferably intranasal administration and oral inhalation. An individual in need thereof The phrase ‘an individual in need thereof’, as used herein, includes reference to a mammal such as a human that benefits from a specified therapy. A treatment method of the invention may be used prophylactically, the exhibition of symptoms or indications for coronavirus infection are not required. Individuals that are especially in need of the method or antibody for use of the invention, are individuals with an elevated risk of coronavirus infection, individuals with an elevated risk of developing severe symptoms (illness), for example COVID-19, and / or individuals with an elevated risk of dying from COVID-19. The person skilled in the art is aware of the risk factors for an elevated risk of coronavirus infection, an elevated risk of developing severe symptoms of coronavirus infection, and an elevated risk of dying from coronavirus infection. Antibody The term ‘antibody’, as used herein, includes reference to an intact immunoglobulin, including monoclonal antibodies, such as chimeric, humanized or human monoclonal antibodies, or to a binding molecule comprising an antigen-binding domain (such as heavy chain CDRs 1-3 of a variable domain) of an antibody as disclosed herein or an antibody that competes with an antibody as disclosed herein for specific binding to the binding partner of the immunoglobulin. In other words, functional fragments of antibodies are also encompassed by the term ‘antibody’. Antibodies are generally Y-shaped proteins. Within the antibody, constant domain and variable domains are generally present. The variable domain facilitates antigen binding. An antibody generally comprises two heavy chains and two light chains. Both the heavy chains and the light chains are partially constant and partially variable. Antibodies occur in a few classes: IgA, IgD, IgE, IgG and IgM. Preferably, the antibody of the invention is of the IgG, preferably IgG1, class. Some classes may 47ressurr subdivided into subclasses or isotypes. For example, the IgG class is subdivided into the subclasses IgG1, IgG2, IgG3 and IgG4. Preferably, the antibody of the invention is of the IgG, preferably IgG1, class. Antigen-binding regions, or antigen-binding fragments of an antibody, which are encompassed by the term ‘antibody’ and which are therefore part of the present invention, may include, for example, Fab, F(ab’), F(ab’)2, dAb, Fv, Fd, CDR fragments, diabodies, triabodies, tetrabodies, single-chain antibodies (scFv, scFv-Fc), bivalent single-chain antibodies, single-chain phage antibodies, (poly)peptides that contain at least a fragment of an immunoglobulin that is sufficient to confer specific antigen binding to the (poly)peptide, etc. The above fragments may be produced synthetically or by enzymatic or chemical cleavage of intact immunoglobulins or they may be genetically engineered by recombinant DNA techniques. The methods for production of antibodies and antigen-binding fragments are well-known to a person skilled in the art. The antibody may be conjugated or unconjugated. The antibody may be conjugated, linked, or otherwise physically or functionally associated with an effector moiety or tag, such as inter alia an enzyme, a liposome, a radioactive substance, a fluorophore, a toxic substance. Antibodies may have been stabilized, multimerized, humanized or otherwise manipulated. Antibodies comprise complementarity determining regions situated on the variable domains of the heavy chain and the light chain. The CDRs contribute to a large extent to the antigen binding site. Three CDRs can be distinguished, namely CDR1, CDR2 and CDR3. As each CDR can be located on either the light chain or the heavy chain, there are generally six CDRs for each antigen receptor that collectively contact the antigen: the light chain CDR1, the light chain CDR2, the light chain CDR3, the heavy chain CDR1, the heavy chain CDR2 and the heavy chain CDR3. The CDRs of type CDR3 are the most variable. The CDRs can be specific for linear epitopes, discontinuous epitopes, or conformational epitopes of proteins or protein fragments, either as present on the protein in its native conformation or, in some cases, as present on the proteins as denatured or activated. Epitopes may also consist of or comprise post-translational modifications of proteins. Antibodies of the invention that are of particular interest, are antibodies comprising CDRs that recognize coronavirus antigens, such as the spike protein and in particular the fusion peptide of the spike protein. The antibody as disclosed herein binds to a conserved epitope in the fusion peptide at the base of the spike protein of the SARS- CoV-2 virion. The epitope of the antibody as disclosed herein uses light and heavy chain CDR loops. The antibody as disclosed herein can be used in isolated or non-isolated form. Preferably, the compositions of the invention comprise a single anti-coronavirus antibody as disclosed herein. Preferably, the antibody of the invention as disclosed herein can cross-neutralize coronavirus, in particular SARS-CoV-2. Furthermore, the antibody as disclosed herein can be used alone or in a mixture comprising the antibody (or variant, fragment or bispecific thereof) as disclosed herein, and / or with other antibodies that bind to a coronavirus and have a coronavirus inhibiting effect. In other words, the antibody as disclosed herein can be used in combination, e.g., as a pharmaceutical composition or co-administration of compositions comprising two or more antibodies that specifically bind coronavirus. For example, antibodies having different, but complementary activities can be combined in a single therapy to achieve a desired therapeutic or prophylactic effect, but alternatively, antibodies having identical activities can also be combined in a single therapy to achieve a desired prophylactic or therapeutic effect. Optionally, the mixture further comprises at least one other therapeutic agent. Preferably, the antibody as disclosed herein are a bispecific antibody and / or an antigen binding fragment thereof, wherein the bispecific antibody is capable of binding to the stem helix of a coronavirus and / or capable of binding to fusion peptide of coronavirus. The phrase “capable of binding” encompasses the phase “specifically binds to”, in other words, an antibody, a bispecific antibody and / or an antigen binding fragment thereof as disclosed herein are that is capable of binding to an epitope may also be capable of binding the other epitopes. Preferably, the coronavirus as described herein includes SARS-CoV-2 and variants. The phrase “are replaced by each other”, “are mutually interchanged”, “swap places with each other”, or “are traded for one another” as used herein, includes reference to at least a part of the heavy chain domains of an antibody or an antigen-binding fragment as described herein such as when a CH1 and / or VH, is substituted by at least a part of the light chain domains such as CL and / or VL to which said at least a part of the heavy chain domains are paired, and at the same instant, said at least a part of the light chain domains is substituted by said at least a part of the heavy chain domains. The phrase “are replaced by each other”, “are mutually interchanged”, “swap places with each other”, or “are traded for one another” are to be used interchangeably herein. Preferably, the antibody as disclosed herein is a human antibody. Framework regions Antibodies also comprise framework regions, generally four framework regions (FR1, FR2, FR3 and FR4) on each of the variable heavy chain domain and variable light chain domain. The CDRs are situated between the framework regions (preferably in the order FR1-CDR1-FR2-CDR2-FR3-CDR3-FR4) and both the CDRs and framework regions together define a heavy chain variable domain (or region) and light chain variable domain (or region) which may also be referred to as an antigen-binding region or domain. Antibodies may be neutralizing, which includes reference to inhibition of a virus as measured by an in vitro neutralization assay, for instance in terms of viral host cell entry and / or viral replication. Neutralization can for example be achieved by inhibiting the attachment or adhesion of the virus to the cell surface, or by inhibition of the fusion of viral and cellular membranes following attachment of the virus to the target cell or by inhibiting viral egress from cells. Neutralization does not specify the method of neutralization. Preferably, the antibody is cross-neutralizing, which includes reference to the ability of the antibodies of the invention to bind a set of different molecules, preferably different molecules of different subtypes belonging to the Coronaviridae family. The term “domain” or “region” as used herein, with reference to a part of an antibody, bispecific antibody, or an antigen binding fragment thereof, can be used interchangeably herein. The phrase “antigen-binding fragments”, “antigen binding fragments”, “antigen fragment”, “a fragment of an antibody” or “antigen-binding molecule” as used herein, means a protein, polypeptide or molecular complex comprising or consisting of at least one complementarity determining region (CDR) that alone, or in combination with one or more additional CDRs and / or framework regions (FRs), as described herein, is capable of binding to a part of an antigen, including the stem helix of a coronavirus, in particular SARS-CoV-2, and / or the stem helix of a coronavirus, in particular SARS-CoV-2 and its variants of concern. The phrases “antigen-binding fragments”, “antigen binding fragments”, “antigen fragment”, “a fragment of an antibody” or “antigen-binding molecule” as used herein, can be used interchangeably. For instance, the phrase “antigen binding fragments” as used herein is to be used interchangeably with the phrase “antibody fragments” as used herein. Preferably, the antibody of the invention as disclosed herein can cross-neutralize coronavirus, in particular SARS-CoV-2. IgG antibody The term ‘IgG antibody’, as used herein, includes reference to an antibody comprising two antigen-binding sites. IgG is the most common antibody in human serum. Heavy chains of IgG antibodies are of type γ, which can be subdivided in γ1, γ2, γ3 and γ4. Preferably, the antibodies described herein are γ1 heavy chains. Light chains of IgG antibodies are of type λ or κ. Preferably, the antibodies described herein are λ light chains. Preferably, the antibody is an IgG antibody, preferably an IgG1 antibody. IgA antibody The term ‘IgA antibody’, as used herein, includes reference to an antibody comprising two to four antigen-binding sites. IgA is the most abundant antibody in mucosal secretions. An IgA antibody can be produced in monomeric, dimeric or secretory form, with two or four antigen-binding sites, respectively, and can exist as an IgA1 or IgA2 isotype. [Heavy chains of IgA antibodies are of type α, which can be subdivided in α1 and α2. Light chains of IgA antibodies are of type λ or κ. Preferably, the antibody is an IgA antibody. IgM antibody The term ‘IgM antibody’, as used herein, includes reference to an antibody comprising ten to twelve antigen-binding sites. An IgM antibody can be produced in pentameric or hexameric form. Heavy chains of IgM antibodies are of type µ. Light chains of IgM antibodies are of type λ or κ. Preferably, the antibody is an IgM antibody. Anti-Coronavirus antibody The term ‘anti-coronavirus antibody’, as used herein, includes reference to an antibody as disclosed herein, i.e. an antibody that can be used in a treatment method of the invention. Preferably, the anti-coronavirus antibody of the invention is able to treat different subtypes of coronavirus. For the avoidance of doubt, the term ‘anti-coronavirus antibody’, can be used interchangeably with ‘coronavirus antibody’. A composition In a preferred embodiment, an antibody disclosed herein is the sole active ingredient in a composition administered for treatment, e.g., the antibody is provided in a composition as the sole active ingredient. In a preferred embodiment, the active ingredients comprise an antibody disclosed herein, e.g., the antibody is provided either as a composition as the sole active ingredient in a composition administered for treatment or in a combination with another antibody. Preferably, the composition of the invention is a water-based composition such as an aqueous liquid. Preferably, the composition of the invention further comprises one or more salts, for example sodium chloride. The composition of the invention may further comprise one or more buffering agents, for example sodium acetate. The composition of the invention may further comprise one or more carbohydrates, such as sucrose, or other active ingredients, such as other antibodies, neuraminidase inhibitors, endonuclease inhibitors, and adjuvants such as oils, cytokines, emulsifiers, or combinations thereof. The pH of the composition of the invention can be between 4 and 8, more preferably the pH is around 5.5. Preferably the pH is around 7.4. Mucosal composition The term ‘mucosal composition’, as used herein, refers to any pharmaceutical formulation that may be topically applied to a mucosal surface and delays or resists the mucosal flushing or removal action. The term ‘mucosal composition’, may be used in reference to a route of administration in which an antibody, as disclosed herein, is provided into the nasal cavity, oropharyngeal region or upper respiratory tract, preferably through the nostrils, as part of a prophylactic and / or therapeutic treatment as disclosed herein. Mucosally The mucosa comprises membranes that line cavities in the human body, covering internal organs, and consist of one or more layers of epithelial cells and loose connective tissue, which may produce mucus. The term ‘mucosally’, as used herein, may also be referred to as ‘mucosal administration’, and includes reference to a route of administration in which a drug is prophylactically and / or therapeutically provided to the mucosa, for example, mucosa found in the nose, mouth, lungs, vagina, rectum or stomach. The mucous membrane lubricates and protects these organs and cavities from abrasive particles and bodily fluids, as well as invasive pathogens. Preferably, the antibodies of the invention are administered mucosally. Intranasally The term ‘intranasally’, as used herein, may also be referred to as ‘nasal administration’, and includes reference to a route of administration in which a drug is provided into the upper respiratory tract and / or lower respiratory tract, preferably through the nostrils, as part of a prophylactic and / or therapeutic treatment as disclosed herein. Preferably, the administration provides for drug in the nasal cavity. The back section of the nasal cavity is53ressed to as the pharynx. Nasal administration preferably provides for delivery of antibodies as disclosed herein in the mucous membrane lining the nasal cavity. Intranasal administration can be performed using, for instance, a nasal spray or nose drops. In some embodiments, the drug is delivered to the nasal cavity via the oral route. For example, RetroNose uses a breath-actuated 53ressurized metered-dose inhaler (pMDI) to administer drugs through the buccal cavity during the nasal expiratory phase. Such methods allow the drug particles to enter the nasal cavities through the pharynx. Preferably, the antibodies of the invention are administered intranasally. With intranasal administration, a drug is provided through the nostrils to the upper respiratory tract as part of a prophylactic and / or therapeutic treatment as disclosed herein. Preferably, the administration provides for drug in the nasal cavity. Nasal administration can either be a form of topical administration or systemic administration, as the drugs thus locally delivered can go on to have either local or systemic effects. In the present case, with antibodies as disclosed herein, nasal administration is preferably a form of topical administration. Intranasal administration as disclosed herein may be done using a medicament in liquid form, preferably in the form of drops or nasal spray. The aqueous liquid may comprise adjuvants. These adjuvants may for example be salts, oils, cytokines, emulsifiers, buffering agents, carbohydrates and combinations thereof. Intranasal administration may also be done using a medicament in solid form, such as powders. Oral inhalation The term ‘oral inhalation’, as used herein, may also be referred to as ‘mouth inhalation’, and includes reference to a route of administration in which a drug is provided through the mouth to the upper and / or lower respiratory tract such as lungs, as part of a prophylactic and / or therapeutic treatment of the invention. Oral inhalation may for example be applied for drugs in their powdered form and drugs in the form of liquid droplets or aerosols. Preferably, the antibodies of the invention are administered by oral inhalation. With oral inhalation, a drug is provided through the mouth to the respiratory tract, preferably lower respiratory tract such as lungs, as part of a prophylactic and / or therapeutic treatment of the invention. As described further herein, oral inhalation also includes nasal drug delivery (also referred to as nasal drug delivery via the oral route). Oral inhalation may for example be applied for drugs in their powdered form and drugs in the form of liquid droplets or aerosols. Oral inhalation may include the use of an inhaler. The inhaler may be involved in the achievement of the dose that was determined. The drug that is administered by oral inhalation may reach the lung but may also partially be cleared out by exhalation. Administration by oral inhalation as disclosed herein may be done using a medicament comprising aerosols in powdered (solid) or liquid form. Powdered aerosols comprising particles smaller than 3 µm in diameter will primarily reach the respiratory region of the lung, and will therefore be absorbed better than larger particles. The medicament may comprise adjuvants. These adjuvants may for example be salts, oils, cytokines, emulsifiers, buffering agents, carbohydrates and combinations thereof. Oropharyngeal administration The term ‘oropharyngeal administration’, as used herein, may also be referred to as delivery to the part of the pharynx that lies between the soft palate and the hyoid bone and includes reference to a route of administration in which a drug is provided via either the mouth or nasal passages as part of a prophylactic and / or therapeutic treatment. Oropharyngeal administration may, for example, be used for drugs in their powdered form and drugs in the form of liquid droplets or aerosols. Preferably, the antibodies of the invention are administered by oropharyngeal administration. Prior to The term ‘prior to’, as used herein, includes reference to the administration of an antibody before an individual has been exposed to, or is infected with, a coronavirus. Preferably, the antibody as disclosed is administered to an individual up to 24 hours prior to coronavirus exposure, for example between zero and 24 hours before the individual has been exposed to said coronavirus. Preferably, the antibody as disclosed is administered to an individual up to 48 hours prior to coronavirus exposure, for example between zero and 48 hours before the individual has been exposed to said coronavirus. In a preferred embodiment, the antibody is administered 2 days or more prior to coronavirus exposure. In a preferred embodiment, the antibody is administered 3 days or more prior to coronavirus exposure. In a preferred embodiment, the antibody is administered 4 days, or more prior to coronavirus exposure. In a preferred embodiment, the antibody is administered 5 days or more prior to coronavirus exposure. In a preferred embodiment, the antibody is administered 6 days or more prior to coronavirus exposure. In a preferred embodiment, the antibody is administered 7 days or more prior to coronavirus exposure. Dosage The term ‘dosage’ as used herein, refers to the amount of antibody to be given at a particular time (e.g., over the course of a 24-hour, 12-hour, 30-minute period, etc.). A dose refers to a single dosing episode, whether the dose is a unit dosage form or multiple unit dosage forms taken together (e.g., ingestion of two or more pills, receiving two or more nasal administrations). A dosage includes reference to a pharmaceutical dosage form wherein the medicament is packaged for administration as, e.g., a single-unit dose or multiple-unit dose. A dosage may also be administered as, e.g., one or more drops of an antibody-comprising composition (e.g., nasal drops) or one or more sprays of an antibody- comprising composition (e.g., nasal sprays). Preferably, a suitable dosage of an antibody as disclosed herein contains a dose of between 0.01 mg and 20 mg, preferably 0.1 mg and 15 mg, more preferably around 0.5 mg and 10 mg or even around 1 mg, e.g. when the dosage is for intranasal administration. Such dosages are also referred to as “flat dosages” or “nominal dosages” in contrast to dosages based on the weight of the patient. Flat dosages have the advantage that the medicament can be packaged in a single-unit dose, for example. A single dose of an antibody according to the present invention can provide protection from coronavirus infection for several days and may be provided “on demand” or “as needed”. For example, an individual may administer antibody before leaving the house or before coming into contact with other individuals. In order to provide long-lasting protection, the antibody may be administered on a regular basis. For example, the antibody is administered once, or at least once per month. In a preferred embodiment, the antibody is administered once, or at least once per week, e.g., twice weekly. In a preferred embodiment, the antibody is administered once, or at least once per day. As is clear to a skilled person, less antibody may be administered when the antibody is administered more frequently (e.g., daily). In a preferred embodiment, between 0.01 mg to 20 mg of antibody is administered per week (e.g., once or twice weekly or daily). In an exemplary embodiment, between 0.1 mg and 25 mg is administered daily (i.e. between 0.7 mg and 175 mg per week). In an exemplary embodiment, 0.5 mg to 3.5 mg is administered daily (i.e. between 3.5 mg and 24.5 mg per week). The invention also provides a composition formulated for intranasal administration and / or oral inhalation comprising an antibody as disclosed herein, preferably in a single dose unit between 0.1 mg to 20 mg, preferably 0.5 mg to 15 mg or preferably 1 mg to 12.5 mg. Use in a method for treatment The present invention relates inter alia to an antibody as disclosed herein, for use in a method for treatment of coronavirus infection in an individual, more specifically the antibody can be used in a method for the prophylactic and / or therapeutic treatment of coronavirus infection in an individual. Complementarity-determining regions (CDRs) Preferably, the CDR regions are identified according to Kabat et al. (1991) as described in Sequences of Proteins of Immunological Interest. In a preferred embodiment, the binding interaction of the binding molecules, preferably the antibody, and the fusion peptide is mediated exclusively by light and heavy chain variable sequences. The antibody as disclosed herein may be capable of specifically binding to a coronavirus that is in attenuated or inactivated form or that is viable, and / or in an infective form. The antibody as disclosed herein is also capable of specifically binding to one or more fragments of the coronavirus. An antibody as disclosed herein comprises a preferred heavy chain CDR1 sequence comprising any one of the following SEQ ID NO: 006 to 011, 013 to 018, 022 to 027, 033 to 038, 053 to 058, 063 to 068. A CDR comprising the amino acid sequence SEQ ID NO: 013 is especially preferred. An antibody as disclosed herein comprises a preferred heavy chain CDR2 sequence comprising any one of the following SEQ ID NO: 082 to 087, 093 to 098, 115 to 120, 126 to 131, 170 to 175, 191 to 196. A CDR comprising the amino acid sequence SEQ ID NO: 170 is especially preferred. An antibody as disclosed herein comprises a preferred heavy chain CDR3 sequence comprising any one of the following SEQ ID NO: 202 to 207, 213 to 218, 266 to 271, 277 to 282, 299 to 304, 310 to 315. A CDR comprising the amino acid sequence SEQ ID NO: 266 is especially preferred. An antibody as disclosed herein comprises a preferred light chain CDR1 sequence comprising any one of the following SEQ ID NO: 321 to 326, 353 to 358, 364 to 369, 386 to 391, 408 to 413, 430 to 435. A CDR comprising the amino acid sequence SEQ ID NO: 386 is especially preferred. An antibody as disclosed herein comprises a preferred light chain CDR2 sequence comprising any one of the following SEQ ID NO: 439 to 444, 450 to 455, 461 to 466, 472 to 477, 489 to 494, 523 to 528. A CDR comprising the amino acid sequence SEQ ID NO: 439 is especially preferred. An antibody as disclosed herein comprises a preferred light chain CDR3 sequence comprising any one of the following SEQ ID NO: 534 to 539, 545 to 550, 556 to 561, 584 to 589, 613 to 618, 634 to 639. A CDR comprising the amino acid sequence SEQ ID NO: 584 is especially preferred. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a heavy chain framework region FR1 of SEQ ID NO: 642. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a heavy chain framework region FR2 of SEQ ID NO: 643. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a heavy chain framework region FR3 of SEQ ID NO: 644. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a heavy chain framework region FR4 of SEQ ID NO: 645. In a preferred embodiment, the heavy chain variable domain of said antibody comprises – a heavy chain framework region FR1 of SEQ ID NO: 642, a heavy chain framework region FR2 of SEQ ID NO: 643, a heavy chain framework region FR3 of SEQ ID NO: 644, and / or a heavy chain framework region FR4 of SEQ ID NO: 645, preferably all said heavy chain heavy chain framework regions FR1 to FR4. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a light chain framework region FR1 of SEQ ID NO: 646. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a light chain framework region FR2 of SEQ ID NO: 647. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a light chain framework region FR3 of SEQ ID NO: 648. An antibody as disclosed herein comprises a heavy chain variable domain that further comprises at least a light chain framework region FR4 of SEQ ID NO: 649. In a preferred embodiment, the light chain variable domain of said antibody comprises – a heavy chain framework region FR1 of SEQ ID NO: 646, a light chain framework region FR2 of SEQ ID NO: 647, a light chain framework region FR3 of SEQ ID NO: 648, and / or a light chain framework region FR4 of SEQ ID NO: 649, preferably all said light chain framework regions are FR1 to FR4. Most preferably, an antibody as disclosed herein comprises a heavy chain variable domain having the sequence of SEQ ID NO: 640 and / or a light chain variable domain having the sequence of SEQ ID NO: 641. In treatment methods of the invention, the heavy chain variable domain (VH) of the antibody is preferably indicated as SEQ ID NO:640. In treatment methods or compositions of the invention, the light chain variable domain (VL) of the antibody is preferably indicated as SEQ ID NO:641. In treatment methods or compositions of the invention, the antibody can be an antibody as disclosed herein, or a binding molecule comprising an antigen-binding domain such as a variable domain (V) thereof. Preferably, an antibody as disclosed herein comprises a heavy chain variable domain having the sequence of SEQ ID NO:640 having at most 15, preferably 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10, more preferably having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions. Preferably, an antibody as disclosed herein comprises a light chain variable domain having the sequence of SEQ ID NO:641 having at most 15, preferably 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10, more preferably having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions. Preferably, said amino acid insertions, deletions, substitutions in respect of either the heavy chain variable domain and / or the light chain variable domain are not in the CDRs.

[0002] SEQUENCES CDRs and framework regions defined herein are based on the Kabat numbering scheme as described in Sequences of Proteins of Immunological Interest (Kabat et al., 1991). Heavy chain CDR1 region (SEQ ID NO:001 to SEQ ID NO:076) SEQ ID NO.: 001 DTFS SEQ ID NO.: 002 DTFSD SEQ ID NO.: 003 DTFSDY SEQ ID NO.: 004 DTFSDYR SEQ ID NO.: 005 DTFSDYRI SEQ ID NO.: 006 DTFSDYRIH SEQ ID NO.: 007 DTFSDYRIHW SEQ ID NO.: 008 DTFSDYRIHWV SEQ ID NO.: 009 DTFSDYRIHWVR SEQ ID NO.: 010 DTFSDYRIHWVRQ SEQ ID NO.: 011 DTFSDYRIHWVRQA SEQ ID NO.: 012 DYRI SEQ ID NO.: 013 DYRIH SEQ ID NO.: 014 DYRIHW SEQ ID NO.: 015 DYRIHWV SEQ ID NO.: 016 DYRIHWVR SEQ ID NO.: 017 DYRIHWVRQ SEQ ID NO.: 018 DYRIHWVRQA SEQ ID NO.: 019 FSDY SEQ ID NO.: 020 FSDYR SEQ ID NO.: 021 FSDYRI SEQ ID NO.: 022 FSDYRIH SEQ ID NO.: 023 FSDYRIHW SEQ ID NO.: 024 FSDYRIHWV SEQ ID NO.: 025 FSDYRIHWVR SEQ ID NO.: 026 FSDYRIHWVRQ SEQ ID NO.: 027 FSDYRIHWVRQA SEQ ID NO.: 028 GDTFS SEQ ID NO.: 029 GDTFSD SEQ ID NO.: 030 GDTFSDY SEQ ID NO.: 031 GDTFSDYR SEQ ID NO.: 032 GDTFSDYRI SEQ ID NO.: 033 GDTFSDYRIH SEQ ID NO.: 034 GDTFSDYRIHW SEQ ID NO.: 035 GDTFSDYRIHWV SEQ ID NO.: 036 GDTFSDYRIHWVR SEQ ID NO.: 037 GDTFSDYRIHWVRQ SEQ ID NO.: 038 GDTFSDYRIHWVRQA SEQ ID NO.: 039 HWVR SEQ ID NO.: 040 HWVRQ SEQ ID NO.: 041 HWVRQA SEQ ID NO.: 042 IHWV SEQ ID NO.: 043 IHWVR SEQ ID NO.: 044 IHWVRQ SEQ ID NO.: 045 IHWVRQA SEQ ID NO.: 046 RIHW SEQ ID NO.: 047 RIHWV SEQ ID NO.: 048 RIHWVR SEQ ID NO.: 049 RIHWVRQ SEQ ID NO.: 050 RIHWVRQA SEQ ID NO.: 051 SDYR SEQ ID NO.: 052 SDYRI SEQ ID NO.: 053 SDYRIH SEQ ID NO.: 054 SDYRIHW SEQ ID NO.: 055 SDYRIHWV SEQ ID NO.: 056 SDYRIHWVR SEQ ID NO.: 057 SDYRIHWVRQ SEQ ID NO.: 058 SDYRIHWVRQA SEQ ID NO.: 059 TFSD SEQ ID NO.: 060 TFSDY SEQ ID NO.: 061 TFSDYR SEQ ID NO.: 062 TFSDYRI SEQ ID NO.: 063 TFSDYRIH SEQ ID NO.: 064 TFSDYRIHW SEQ ID NO.: 065 TFSDYRIHWV SEQ ID NO.: 066 TFSDYRIHWVR SEQ ID NO.: 067 TFSDYRIHWVRQ SEQ ID NO.: 068 TFSDYRIHWVRQA SEQ ID NO.: 069 WVRQ SEQ ID NO.: 070 WVRQA SEQ ID NO.: 071 YRIH SEQ ID NO.: 072 YRIHW SEQ ID NO.: 073 YRIHWV SEQ ID NO.: 074 YRIHWVR SEQ ID NO.: 075 YRIHWVRQ SEQ ID NO.: 076 YRIHWVRQA Heavy chain CDR2 region (SEQ ID NO:077 to SEQ ID NO:196) SEQ ID NO.: 077 EWMGRMNPKSGDTNFA SEQ ID NO.: 078 EWMGRMNPKSGDTNFAQ SEQ ID NO.: 079 EWMGRMNPKSGDTNFAQK SEQ ID NO.: 080 EWMGRMNPKSGDTNFAQKF SEQ ID NO.: 081 EWMGRMNPKSGDTNFAQKFQ SEQ ID NO.: 082 EWMGRMNPKSGDTNFAQKFQG SEQ ID NO.: 083 EWMGRMNPKSGDTNFAQKFQGR SEQ ID NO.: 084 EWMGRMNPKSGDTNFAQKFQGRV SEQ ID NO.: 085 EWMGRMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 086 EWMGRMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 087 EWMGRMNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 088 GRMNPKSGDTNFA SEQ ID NO.: 089 GRMNPKSGDTNFAQ SEQ ID NO.: 090 GRMNPKSGDTNFAQK SEQ ID NO.: 091 GRMNPKSGDTNFAQKF SEQ ID NO.: 092 GRMNPKSGDTNFAQKFQ SEQ ID NO.: 093 GRMNPKSGDTNFAQKFQG SEQ ID NO.: 094 GRMNPKSGDTNFAQKFQGR SEQ ID NO.: 095 GRMNPKSGDTNFAQKFQGRV SEQ ID NO.: 096 GRMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 097 GRMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 098 GRMNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 099 KSGDTNFA SEQ ID NO.: 100 KSGDTNFAQ SEQ ID NO.: 101 KSGDTNFAQK SEQ ID NO.: 102 KSGDTNFAQKF SEQ ID NO.: 103 KSGDTNFAQKFQ SEQ ID NO.: 104 KSGDTNFAQKFQG SEQ ID NO.: 105 KSGDTNFAQKFQGR SEQ ID NO.: 106 KSGDTNFAQKFQGRV SEQ ID NO.: 107 KSGDTNFAQKFQGRVT SEQ ID NO.: 108 KSGDTNFAQKFQGRVTM SEQ ID NO.: 109 KSGDTNFAQKFQGRVTMT SEQ ID NO.: 110 LEWMGRMNPKSGDTNFA SEQ ID NO.: 111 LEWMGRMNPKSGDTNFAQ SEQ ID NO.: 112 LEWMGRMNPKSGDTNFAQK SEQ ID NO.: 113 LEWMGRMNPKSGDTNFAQKF SEQ ID NO.: 114 LEWMGRMNPKSGDTNFAQKFQ SEQ ID NO.: 115 LEWMGRMNPKSGDTNFAQKFQG SEQ ID NO.: 116 LEWMGRMNPKSGDTNFAQKFQGR SEQ ID NO.: 117 LEWMGRMNPKSGDTNFAQKFQGRV SEQ ID NO.: 118 LEWMGRMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 119 LEWMGRMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 120 LEWMGRMNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 121 MGRMNPKSGDTNFA SEQ ID NO.: 122 MGRMNPKSGDTNFAQ SEQ ID NO.: 123 MGRMNPKSGDTNFAQK SEQ ID NO.: 124 MGRMNPKSGDTNFAQKF SEQ ID NO.: 125 MGRMNPKSGDTNFAQKFQ SEQ ID NO.: 126 MGRMNPKSGDTNFAQKFQG SEQ ID NO.: 127 MGRMNPKSGDTNFAQKFQGR SEQ ID NO.: 128 MGRMNPKSGDTNFAQKFQGRV SEQ ID NO.: 129 MGRMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 130 MGRMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 131 MGRMNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 132 MNPKSGDTNFA SEQ ID NO.: 133 MNPKSGDTNFAQ SEQ ID NO.: 134 MNPKSGDTNFAQK SEQ ID NO.: 135 MNPKSGDTNFAQKF SEQ ID NO.: 136 MNPKSGDTNFAQKFQ SEQ ID NO.: 137 MNPKSGDTNFAQKFQG SEQ ID NO.: 138 MNPKSGDTNFAQKFQGR SEQ ID NO.: 139 MNPKSGDTNFAQKFQGRV SEQ ID NO.: 140 MNPKSGDTNFAQKFQGRVT SEQ ID NO.: 141 MNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 142 MNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 143 NPKSGDTNFA SEQ ID NO.: 144 NPKSGDTNFAQ SEQ ID NO.: 145 NPKSGDTNFAQK SEQ ID NO.: 146 NPKSGDTNFAQKF SEQ ID NO.: 147 NPKSGDTNFAQKFQ SEQ ID NO.: 148 NPKSGDTNFAQKFQG SEQ ID NO.: 149 NPKSGDTNFAQKFQGR SEQ ID NO.: 150 NPKSGDTNFAQKFQGRV SEQ ID NO.: 151 NPKSGDTNFAQKFQGRVT SEQ ID NO.: 152 NPKSGDTNFAQKFQGRVTM SEQ ID NO.: 153 NPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 154 PKSGDTNFA SEQ ID NO.: 155 PKSGDTNFAQ SEQ ID NO.: 156 PKSGDTNFAQK SEQ ID NO.: 157 PKSGDTNFAQKF SEQ ID NO.: 158 PKSGDTNFAQKFQ SEQ ID NO.: 159 PKSGDTNFAQKFQG SEQ ID NO.: 160 PKSGDTNFAQKFQGR SEQ ID NO.: 161 PKSGDTNFAQKFQGRV SEQ ID NO.: 162 PKSGDTNFAQKFQGRVT SEQ ID NO.: 163 PKSGDTNFAQKFQGRVTM SEQ ID NO.: 164 PKSGDTNFAQKFQGRVTMT SEQ ID NO.: 165 RMNPKSGDTNFA SEQ ID NO.: 166 RMNPKSGDTNFAQ SEQ ID NO.: 167 RMNPKSGDTNFAQK SEQ ID NO.: 168 RMNPKSGDTNFAQKF SEQ ID NO.: 169 RMNPKSGDTNFAQKFQ SEQ ID NO.: 170 RMNPKSGDTNFAQKFQG SEQ ID NO.: 171 RMNPKSGDTNFAQKFQGR SEQ ID NO.: 172 RMNPKSGDTNFAQKFQGRV SEQ ID NO.: 173 RMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 174 RMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 175 RMNPKSGDTNFAQKFQGRVTMT SEQ ID NO.: 176 SGDTNFAQ SEQ ID NO.: 177 SGDTNFAQK SEQ ID NO.: 178 SGDTNFAQKF SEQ ID NO.: 179 SGDTNFAQKFQ SEQ ID NO.: 180 SGDTNFAQKFQG SEQ ID NO.: 181 SGDTNFAQKFQGR SEQ ID NO.: 182 SGDTNFAQKFQGRV SEQ ID NO.: 183 SGDTNFAQKFQGRVT SEQ ID NO.: 184 SGDTNFAQKFQGRVTM SEQ ID NO.: 185 SGDTNFAQKFQGRVTMT SEQ ID NO.: 186 WMGRMNPKSGDTNFA SEQ ID NO.: 187 WMGRMNPKSGDTNFAQ SEQ ID NO.: 188 WMGRMNPKSGDTNFAQK SEQ ID NO.: 189 WMGRMNPKSGDTNFAQKF SEQ ID NO.: 190 WMGRMNPKSGDTNFAQKFQ SEQ ID NO.: 191 WMGRMNPKSGDTNFAQKFQG SEQ ID NO.: 192 WMGRMNPKSGDTNFAQKFQGR SEQ ID NO.: 193 WMGRMNPKSGDTNFAQKFQGRV SEQ ID NO.: 194 WMGRMNPKSGDTNFAQKFQGRVT SEQ ID NO.: 195 WMGRMNPKSGDTNFAQKFQGRVTM SEQ ID NO.: 196 WMGRMNPKSGDTNFAQKFQGRVTMT Heavy chain CDR3 region (SEQ ID NO:197 to SEQ ID NO:315) SEQ ID NO.: 197 ASLLIVGGFDPL SEQ ID NO.: 198 ASLLIVGGFDPLD SEQ ID NO.: 199 ASLLIVGGFDPLDD SEQ ID NO.: 200 ASLLIVGGFDPLDDF SEQ ID NO.: 201 ASLLIVGGFDPLDDFE SEQ ID NO.: 202 ASLLIVGGFDPLDDFEV SEQ ID NO.: 203 ASLLIVGGFDPLDDFEVW SEQ ID NO.: 204 ASLLIVGGFDPLDDFEVWG SEQ ID NO.: 205 ASLLIVGGFDPLDDFEVWGQ SEQ ID NO.: 206 ASLLIVGGFDPLDDFEVWGQG SEQ ID NO.: 207 ASLLIVGGFDPLDDFEVWGQGT SEQ ID NO.: 208 CASLLIVGGFDPL SEQ ID NO.: 209 CASLLIVGGFDPLD SEQ ID NO.: 210 CASLLIVGGFDPLDD SEQ ID NO.: 211 CASLLIVGGFDPLDDF SEQ ID NO.: 212 CASLLIVGGFDPLDDFE SEQ ID NO.: 213 CASLLIVGGFDPLDDFEV SEQ ID NO.: 214 CASLLIVGGFDPLDDFEVW SEQ ID NO.: 215 CASLLIVGGFDPLDDFEVWG SEQ ID NO.: 216 CASLLIVGGFDPLDDFEVWGQ SEQ ID NO.: 217 CASLLIVGGFDPLDDFEVWGQG SEQ ID NO.: 218 CASLLIVGGFDPLDDFEVWGQGT SEQ ID NO.: 219 GFDPLDD SEQ ID NO.: 220 GFDPLDDF SEQ ID NO.: 221 GFDPLDDFE SEQ ID NO.: 222 GFDPLDDFEV SEQ ID NO.: 223 GFDPLDDFEVW SEQ ID NO.: 224 GFDPLDDFEVWG SEQ ID NO.: 225 GFDPLDDFEVWGQ SEQ ID NO.: 226 GFDPLDDFEVWGQG SEQ ID NO.: 227 GFDPLDDFEVWGQGT SEQ ID NO.: 228 GGFDPL SEQ ID NO.: 229 GGFDPLD SEQ ID NO.: 230 GGFDPLDD SEQ ID NO.: 231 GGFDPLDDF SEQ ID NO.: 232 GGFDPLDDFE SEQ ID NO.: 233 GGFDPLDDFEV SEQ ID NO.: 234 GGFDPLDDFEVW SEQ ID NO.: 235 GGFDPLDDFEVWG SEQ ID NO.: 236 GGFDPLDDFEVWGQ SEQ ID NO.: 237 GGFDPLDDFEVWGQG SEQ ID NO.: 238 GGFDPLDDFEVWGQGT SEQ ID NO.: 239 IVGGFDPL SEQ ID NO.: 240 IVGGFDPLD SEQ ID NO.: 241 IVGGFDPLDD SEQ ID NO.: 242 IVGGFDPLDDF SEQ ID NO.: 243 IVGGFDPLDDFE SEQ ID NO.: 244 IVGGFDPLDDFEV SEQ ID NO.: 245 IVGGFDPLDDFEVW SEQ ID NO.: 246 IVGGFDPLDDFEVWG SEQ ID NO.: 247 IVGGFDPLDDFEVWGQ SEQ ID NO.: 248 IVGGFDPLDDFEVWGQG SEQ ID NO.: 249 IVGGFDPLDDFEVWGQGT SEQ ID NO.: 250 LIVGGFDPL SEQ ID NO.: 251 LIVGGFDPLD SEQ ID NO.: 252 LIVGGFDPLDD SEQ ID NO.: 253 LIVGGFDPLDDF SEQ ID NO.: 254 LIVGGFDPLDDFE SEQ ID NO.: 255 LIVGGFDPLDDFEV SEQ ID NO.: 256 LIVGGFDPLDDFEVW SEQ ID NO.: 257 LIVGGFDPLDDFEVWG SEQ ID NO.: 258 LIVGGFDPLDDFEVWGQ SEQ ID NO.: 259 LIVGGFDPLDDFEVWGQG SEQ ID NO.: 260 LIVGGFDPLDDFEVWGQGT SEQ ID NO.: 261 LLIVGGFDPL SEQ ID NO.: 262 LLIVGGFDPLD SEQ ID NO.: 263 LLIVGGFDPLDD SEQ ID NO.: 264 LLIVGGFDPLDDF SEQ ID NO.: 265 LLIVGGFDPLDDFE SEQ ID NO.: 266 LLIVGGFDPLDDFEV SEQ ID NO.: 267 LLIVGGFDPLDDFEVW SEQ ID NO.: 268 LLIVGGFDPLDDFEVWG SEQ ID NO.: 269 LLIVGGFDPLDDFEVWGQ SEQ ID NO.: 270 LLIVGGFDPLDDFEVWGQG SEQ ID NO.: 271 LLIVGGFDPLDDFEVWGQGT SEQ ID NO.: 272 SLLIVGGFDPL SEQ ID NO.: 273 SLLIVGGFDPLD SEQ ID NO.: 274 SLLIVGGFDPLDD SEQ ID NO.: 275 SLLIVGGFDPLDDF SEQ ID NO.: 276 SLLIVGGFDPLDDFE SEQ ID NO.: 277 SLLIVGGFDPLDDFEV SEQ ID NO.: 278 SLLIVGGFDPLDDFEVW SEQ ID NO.: 279 SLLIVGGFDPLDDFEVWG SEQ ID NO.: 280 SLLIVGGFDPLDDFEVWGQ SEQ ID NO.: 281 SLLIVGGFDPLDDFEVWGQG SEQ ID NO.: 282 SLLIVGGFDPLDDFEVWGQGT SEQ ID NO.: 283 VGGFDPL SEQ ID NO.: 284 VGGFDPLD SEQ ID NO.: 285 VGGFDPLDD SEQ ID NO.: 286 VGGFDPLDDF SEQ ID NO.: 287 VGGFDPLDDFE SEQ ID NO.: 288 VGGFDPLDDFEV SEQ ID NO.: 289 VGGFDPLDDFEVW SEQ ID NO.: 290 VGGFDPLDDFEVWG SEQ ID NO.: 291 VGGFDPLDDFEVWGQ SEQ ID NO.: 292 VGGFDPLDDFEVWGQG SEQ ID NO.: 293 VGGFDPLDDFEVWGQGT SEQ ID NO.: 294 YCASLLIVGGFDPL SEQ ID NO.: 295 YCASLLIVGGFDPLD SEQ ID NO.: 296 YCASLLIVGGFDPLDD SEQ ID NO.: 297 YCASLLIVGGFDPLDDF SEQ ID NO.: 298 YCASLLIVGGFDPLDDFE SEQ ID NO.: 299 YCASLLIVGGFDPLDDFEV SEQ ID NO.: 300 YCASLLIVGGFDPLDDFEVW SEQ ID NO.: 301 YCASLLIVGGFDPLDDFEVWG SEQ ID NO.: 302 YCASLLIVGGFDPLDDFEVWGQ SEQ ID NO.: 303 YCASLLIVGGFDPLDDFEVWGQG SEQ ID NO.: 304 YCASLLIVGGFDPLDDFEVWGQGT SEQ ID NO.: 305 YYCASLLIVGGFDPL SEQ ID NO.: 306 YYCASLLIVGGFDPLD SEQ ID NO.: 307 YYCASLLIVGGFDPLDD SEQ ID NO.: 308 YYCASLLIVGGFDPLDDF SEQ ID NO.: 309 YYCASLLIVGGFDPLDDFE SEQ ID NO.: 310 YYCASLLIVGGFDPLDDFEV SEQ ID NO.: 311 YYCASLLIVGGFDPLDDFEVW SEQ ID NO.: 312 YYCASLLIVGGFDPLDDFEVWG SEQ ID NO.: 313 YYCASLLIVGGFDPLDDFEVWGQ SEQ ID NO.: 314 YYCASLLIVGGFDPLDDFEVWGQG SEQ ID NO.: 315 YYCASLLIVGGFDPLDDFEVWGQGT Light chain CDR1 region (SEQ ID NO:316 to SEQ ID NO:435) SEQ ID NO.: 316 CSGTSSDVGG SEQ ID NO.: 317 CSGTSSDVGGY SEQ ID NO.: 318 CSGTSSDVGGYN SEQ ID NO.: 319 CSGTSSDVGGYNF SEQ ID NO.: 320 CSGTSSDVGGYNFV SEQ ID NO.: 321 CSGTSSDVGGYNFVS SEQ ID NO.: 322 CSGTSSDVGGYNFVSW SEQ ID NO.: 323 CSGTSSDVGGYNFVSWY SEQ ID NO.: 324 CSGTSSDVGGYNFVSWYQ SEQ ID NO.: 325 CSGTSSDVGGYNFVSWYQH SEQ ID NO.: 326 CSGTSSDVGGYNFVSWYQHH SEQ ID NO.: 327 DVGGY SEQ ID NO.: 328 DVGGYN SEQ ID NO.: 329 DVGGYNF SEQ ID NO.: 330 DVGGYNFV SEQ ID NO.: 331 DVGGYNFVS SEQ ID NO.: 332 DVGGYNFVSW SEQ ID NO.: 333 DVGGYNFVSWY SEQ ID NO.: 334 DVGGYNFVSWYQ SEQ ID NO.: 335 DVGGYNFVSWYQH SEQ ID NO.: 336 DVGGYNFVSWYQHH SEQ ID NO.: 337 GTSSDVGG SEQ ID NO.: 338 GTSSDVGGY SEQ ID NO.: 339 GTSSDVGGYN SEQ ID NO.: 340 GTSSDVGGYNF SEQ ID NO.: 341 GTSSDVGGYNFV SEQ ID NO.: 342 GTSSDVGGYNFVS SEQ ID NO.: 343 GTSSDVGGYNFVSW SEQ ID NO.: 344 GTSSDVGGYNFVSWY SEQ ID NO.: 345 GTSSDVGGYNFVSWYQ SEQ ID NO.: 346 GTSSDVGGYNFVSWYQH SEQ ID NO.: 347 GTSSDVGGYNFVSWYQHH SEQ ID NO.: 348 ISCSGTSSDVGG SEQ ID NO.: 349 ISCSGTSSDVGGY SEQ ID NO.: 350 ISCSGTSSDVGGYN SEQ ID NO.: 351 ISCSGTSSDVGGYNF SEQ ID NO.: 352 ISCSGTSSDVGGYNFV SEQ ID NO.: 353 ISCSGTSSDVGGYNFVS SEQ ID NO.: 354 ISCSGTSSDVGGYNFVSW SEQ ID NO.: 355 ISCSGTSSDVGGYNFVSWY SEQ ID NO.: 356 ISCSGTSSDVGGYNFVSWYQ SEQ ID NO.: 357 ISCSGTSSDVGGYNFVSWYQH SEQ ID NO.: 358 ISCSGTSSDVGGYNFVSWYQHH SEQ ID NO.: 359 SCSGTSSDVGG SEQ ID NO.: 360 SCSGTSSDVGGY SEQ ID NO.: 361 SCSGTSSDVGGYN SEQ ID NO.: 362 SCSGTSSDVGGYNF SEQ ID NO.: 363 SCSGTSSDVGGYNFV SEQ ID NO.: 364 SCSGTSSDVGGYNFVS SEQ ID NO.: 365 SCSGTSSDVGGYNFVSW SEQ ID NO.: 366 SCSGTSSDVGGYNFVSWY SEQ ID NO.: 367 SCSGTSSDVGGYNFVSWYQ SEQ ID NO.: 368 SCSGTSSDVGGYNFVSWYQH SEQ ID NO.: 369 SCSGTSSDVGGYNFVSWYQHH SEQ ID NO.: 370 SDVGG SEQ ID NO.: 371 SDVGGY SEQ ID NO.: 372 SDVGGYN SEQ ID NO.: 373 SDVGGYNF SEQ ID NO.: 374 SDVGGYNFV SEQ ID NO.: 375 SDVGGYNFVS SEQ ID NO.: 376 SDVGGYNFVSW SEQ ID NO.: 377 SDVGGYNFVSWY SEQ ID NO.: 378 SDVGGYNFVSWYQ SEQ ID NO.: 379 SDVGGYNFVSWYQH SEQ ID NO.: 380 SDVGGYNFVSWYQHH SEQ ID NO.: 381 SGTSSDVGG SEQ ID NO.: 382 SGTSSDVGGY SEQ ID NO.: 383 SGTSSDVGGYN SEQ ID NO.: 384 SGTSSDVGGYNF SEQ ID NO.: 385 SGTSSDVGGYNFV SEQ ID NO.: 386 SGTSSDVGGYNFVS SEQ ID NO.: 387 SGTSSDVGGYNFVSW SEQ ID NO.: 388 SGTSSDVGGYNFVSWY SEQ ID NO.: 389 SGTSSDVGGYNFVSWYQ SEQ ID NO.: 390 SGTSSDVGGYNFVSWYQH SEQ ID NO.: 391 SGTSSDVGGYNFVSWYQHH SEQ ID NO.: 392 SSDVGG SEQ ID NO.: 393 SSDVGGY SEQ ID NO.: 394 SSDVGGYN SEQ ID NO.: 395 SSDVGGYNF SEQ ID NO.: 396 SSDVGGYNFV SEQ ID NO.: 397 SSDVGGYNFVS SEQ ID NO.: 398 SSDVGGYNFVSW SEQ ID NO.: 399 SSDVGGYNFVSWY SEQ ID NO.: 400 SSDVGGYNFVSWYQ SEQ ID NO.: 401 SSDVGGYNFVSWYQH SEQ ID NO.: 402 SSDVGGYNFVSWYQHH SEQ ID NO.: 403 TISCSGTSSDVGG SEQ ID NO.: 404 TISCSGTSSDVGGY SEQ ID NO.: 405 TISCSGTSSDVGGYN SEQ ID NO.: 406 TISCSGTSSDVGGYNF SEQ ID NO.: 407 TISCSGTSSDVGGYNFV SEQ ID NO.: 408 TISCSGTSSDVGGYNFVS SEQ ID NO.: 409 TISCSGTSSDVGGYNFVSW SEQ ID NO.: 410 TISCSGTSSDVGGYNFVSWY SEQ ID NO.: 411 TISCSGTSSDVGGYNFVSWYQ SEQ ID NO.: 412 TISCSGTSSDVGGYNFVSWYQH SEQ ID NO.: 413 TISCSGTSSDVGGYNFVSWYQHH SEQ ID NO.: 414 TSSDVGG SEQ ID NO.: 415 TSSDVGGY SEQ ID NO.: 416 TSSDVGGYN SEQ ID NO.: 417 TSSDVGGYNF SEQ ID NO.: 418 TSSDVGGYNFV SEQ ID NO.: 419 TSSDVGGYNFVS SEQ ID NO.: 420 TSSDVGGYNFVSW SEQ ID NO.: 421 TSSDVGGYNFVSWY SEQ ID NO.: 422 TSSDVGGYNFVSWYQ SEQ ID NO.: 423 TSSDVGGYNFVSWYQH SEQ ID NO.: 424 TSSDVGGYNFVSWYQHH SEQ ID NO.: 425 VTISCSGTSSDVGG SEQ ID NO.: 426 VTISCSGTSSDVGGY SEQ ID NO.: 427 VTISCSGTSSDVGGYN SEQ ID NO.: 428 VTISCSGTSSDVGGYNF SEQ ID NO.: 429 VTISCSGTSSDVGGYNFV SEQ ID NO.: 430 VTISCSGTSSDVGGYNFVS SEQ ID NO.: 431 VTISCSGTSSDVGGYNFVSW SEQ ID NO.: 432 VTISCSGTSSDVGGYNFVSWY SEQ ID NO.: 433 VTISCSGTSSDVGGYNFVSWYQ SEQ ID NO.: 434 VTISCSGTSSDVGGYNFVSWYQH SEQ ID NO.: 435 VTISCSGTSSDVGGYNFVSWYQHH Light chain CDR2 region (SEQ ID NO:436 to SEQ ID NO:528) SEQ ID NO.: 436 EVTK SEQ ID NO.: 437 EVTKR SEQ ID NO.: 438 EVTKRP SEQ ID NO.: 439 EVTKRPS SEQ ID NO.: 440 EVTKRPSG SEQ ID NO.: 441 EVTKRPSGV SEQ ID NO.: 442 EVTKRPSGVP SEQ ID NO.: 443 EVTKRPSGVPD SEQ ID NO.: 444 EVTKRPSGVPDR SEQ ID NO.: 445 ILIYEV SEQ ID NO.: 446 ILIYEVT SEQ ID NO.: 447 ILIYEVTK SEQ ID NO.: 448 ILIYEVTKR SEQ ID NO.: 449 ILIYEVTKRP SEQ ID NO.: 450 ILIYEVTKRPS SEQ ID NO.: 451 ILIYEVTKRPSG SEQ ID NO.: 452 ILIYEVTKRPSGV SEQ ID NO.: 453 ILIYEVTKRPSGVP SEQ ID NO.: 454 ILIYEVTKRPSGVPD SEQ ID NO.: 455 ILIYEVTKRPSGVPDR SEQ ID NO.: 456 IYEV SEQ ID NO.: 457 IYEVT SEQ ID NO.: 458 IYEVTK SEQ ID NO.: 459 IYEVTKR SEQ ID NO.: 460 IYEVTKRP SEQ ID NO.: 461 IYEVTKRPS SEQ ID NO.: 462 IYEVTKRPSG SEQ ID NO.: 463 IYEVTKRPSGV SEQ ID NO.: 464 IYEVTKRPSGVP SEQ ID NO.: 465 IYEVTKRPSGVPD SEQ ID NO.: 466 IYEVTKRPSGVPDR SEQ ID NO.: 467 KILIYEV SEQ ID NO.: 468 KILIYEVT SEQ ID NO.: 469 KILIYEVTK SEQ ID NO.: 470 KILIYEVTKR SEQ ID NO.: 471 KILIYEVTKRP SEQ ID NO.: 472 KILIYEVTKRPS SEQ ID NO.: 473 KILIYEVTKRPSG SEQ ID NO.: 474 KILIYEVTKRPSGV SEQ ID NO.: 475 KILIYEVTKRPSGVP SEQ ID NO.: 476 KILIYEVTKRPSGVPD SEQ ID NO.: 477 KILIYEVTKRPSGVPDR SEQ ID NO.: 478 KRPS SEQ ID NO.: 479 KRPSG SEQ ID NO.: 480 KRPSGV SEQ ID NO.: 481 KRPSGVP SEQ ID NO.: 482 KRPSGVPD SEQ ID NO.: 483 KRPSGVPDR SEQ ID NO.: 484 LIYEV SEQ ID NO.: 485 LIYEVT SEQ ID NO.: 486 LIYEVTK SEQ ID NO.: 487 LIYEVTKR SEQ ID NO.: 488 LIYEVTKRP SEQ ID NO.: 489 LIYEVTKRPS SEQ ID NO.: 490 LIYEVTKRPSG SEQ ID NO.: 491 LIYEVTKRPSGV SEQ ID NO.: 492 LIYEVTKRPSGVP SEQ ID NO.: 493 LIYEVTKRPSGVPD SEQ ID NO.: 494 LIYEVTKRPSGVPDR SEQ ID NO.: 495 PSGV SEQ ID NO.: 496 PSGVP SEQ ID NO.: 497 PSGVPD SEQ ID NO.: 498 PSGVPDR SEQ ID NO.: 499 RPSG SEQ ID NO.: 500 RPSGV SEQ ID NO.: 501 RPSGVP SEQ ID NO.: 502 RPSGVPD SEQ ID NO.: 503 RPSGVPDR SEQ ID NO.: 504 TKRP SEQ ID NO.: 505 TKRPS SEQ ID NO.: 506 TKRPSG SEQ ID NO.: 507 TKRPSGV SEQ ID NO.: 508 TKRPSGVP SEQ ID NO.: 509 TKRPSGVPD SEQ ID NO.: 510 TKRPSGVPDR SEQ ID NO.: 511 VTKR SEQ ID NO.: 512 VTKRP SEQ ID NO.: 513 VTKRPS SEQ ID NO.: 514 VTKRPSG SEQ ID NO.: 515 VTKRPSGV SEQ ID NO.: 516 VTKRPSGVP SEQ ID NO.: 517 VTKRPSGVPD SEQ ID NO.: 518 VTKRPSGVPDR SEQ ID NO.: 519 YEVT SEQ ID NO.: 520 YEVTK SEQ ID NO.: 521 YEVTKR SEQ ID NO.: 522 YEVTKRP SEQ ID NO.: 523 YEVTKRPS SEQ ID NO.: 524 YEVTKRPSG SEQ ID NO.: 525 YEVTKRPSGV SEQ ID NO.: 526 YEVTKRPSGVP SEQ ID NO.: 527 YEVTKRPSGVPD SEQ ID NO.: 528 YEVTKRPSGVPDR Light chain CDR3 region (SEQ ID NO:529 to SEQ ID NO:639) SEQ ID NO.: 529 ADYYCSSYGG SEQ ID NO.: 530 ADYYCSSYGGT SEQ ID NO.: 531 ADYYCSSYGGTN SEQ ID NO.: 532 ADYYCSSYGGTNN SEQ ID NO.: 533 ADYYCSSYGGTNNL SEQ ID NO.: 534 ADYYCSSYGGTNNLL SEQ ID NO.: 535 ADYYCSSYGGTNNLLF SEQ ID NO.: 536 ADYYCSSYGGTNNLLFG SEQ ID NO.: 537 ADYYCSSYGGTNNLLFGG SEQ ID NO.: 538 ADYYCSSYGGTNNLLFGGG SEQ ID NO.: 539 ADYYCSSYGGTNNLLFGGGT SEQ ID NO.: 540 CSSYGG SEQ ID NO.: 541 CSSYGGT SEQ ID NO.: 542 CSSYGGTN SEQ ID NO.: 543 CSSYGGTNN SEQ ID NO.: 544 CSSYGGTNNL SEQ ID NO.: 545 CSSYGGTNNLL SEQ ID NO.: 546 CSSYGGTNNLLF SEQ ID NO.: 547 CSSYGGTNNLLFG SEQ ID NO.: 548 CSSYGGTNNLLFGG SEQ ID NO.: 549 CSSYGGTNNLLFGGG SEQ ID NO.: 550 CSSYGGTNNLLFGGGT SEQ ID NO.: 551 DYYCSSYGG SEQ ID NO.: 552 DYYCSSYGGT SEQ ID NO.: 553 DYYCSSYGGTN SEQ ID NO.: 554 DYYCSSYGGTNN SEQ ID NO.: 555 DYYCSSYGGTNNL SEQ ID NO.: 556 DYYCSSYGGTNNLL SEQ ID NO.: 557 DYYCSSYGGTNNLLF SEQ ID NO.: 558 DYYCSSYGGTNNLLFG SEQ ID NO.: 559 DYYCSSYGGTNNLLFGG SEQ ID NO.: 560 DYYCSSYGGTNNLLFGGG SEQ ID NO.: 561 DYYCSSYGGTNNLLFGGGT SEQ ID NO.: 562 GGTN SEQ ID NO.: 563 GGTNN SEQ ID NO.: 564 GGTNNL SEQ ID NO.: 565 GGTNNLL SEQ ID NO.: 566 GGTNNLLF SEQ ID NO.: 567 GGTNNLLFG SEQ ID NO.: 568 GGTNNLLFGG SEQ ID NO.: 569 GGTNNLLFGGG SEQ ID NO.: 570 GGTNNLLFGGGT SEQ ID NO.: 571 GTNN SEQ ID NO.: 572 GTNNL SEQ ID NO.: 573 GTNNLL SEQ ID NO.: 574 GTNNLLF SEQ ID NO.: 575 GTNNLLFG SEQ ID NO.: 576 GTNNLLFGG SEQ ID NO.: 577 GTNNLLFGGG SEQ ID NO.: 578 GTNNLLFGGGT SEQ ID NO.: 579 SSYGG SEQ ID NO.: 580 SSYGGT SEQ ID NO.: 581 SSYGGTN SEQ ID NO.: 582 SSYGGTNN SEQ ID NO.: 583 SSYGGTNNL SEQ ID NO.: 584 SSYGGTNNLL SEQ ID NO.: 585 SSYGGTNNLLF SEQ ID NO.: 586 SSYGGTNNLLFG SEQ ID NO.: 587 SSYGGTNNLLFGG SEQ ID NO.: 588 SSYGGTNNLLFGGG SEQ ID NO.: 589 SSYGGTNNLLFGGGT SEQ ID NO.: 590 SYGG SEQ ID NO.: 591 SYGGT SEQ ID NO.: 592 SYGGTN SEQ ID NO.: 593 SYGGTNN SEQ ID NO.: 594 SYGGTNNL SEQ ID NO.: 595 SYGGTNNLL SEQ ID NO.: 596 SYGGTNNLLF SEQ ID NO.: 597 SYGGTNNLLFG SEQ ID NO.: 598 SYGGTNNLLFGG SEQ ID NO.: 599 SYGGTNNLLFGGG SEQ ID NO.: 600 SYGGTNNLLFGGGT SEQ ID NO.: 601 TNNL SEQ ID NO.: 602 TNNLL SEQ ID NO.: 603 TNNLLF SEQ ID NO.: 604 TNNLLFG SEQ ID NO.: 605 TNNLLFGG SEQ ID NO.: 606 TNNLLFGGG SEQ ID NO.: 607 TNNLLFGGGT SEQ ID NO.: 608 YCSSYGG SEQ ID NO.: 609 YCSSYGGT SEQ ID NO.: 610 YCSSYGGTN SEQ ID NO.: 611 YCSSYGGTNN SEQ ID NO.: 612 YCSSYGGTNNL SEQ ID NO.: 613 YCSSYGGTNNLL SEQ ID NO.: 614 YCSSYGGTNNLLF SEQ ID NO.: 615 YCSSYGGTNNLLFG SEQ ID NO.: 616 YCSSYGGTNNLLFGG SEQ ID NO.: 617 YCSSYGGTNNLLFGGG SEQ ID NO.: 618 YCSSYGGTNNLLFGGGT SEQ ID NO.: 619 YGGT SEQ ID NO.: 620 YGGTN SEQ ID NO.: 621 YGGTNN SEQ ID NO.: 622 YGGTNNL SEQ ID NO.: 623 YGGTNNLL SEQ ID NO.: 624 YGGTNNLLF SEQ ID NO.: 625 YGGTNNLLFG SEQ ID NO.: 626 YGGTNNLLFGG SEQ ID NO.: 627 YGGTNNLLFGGG SEQ ID NO.: 628 YGGTNNLLFGGGT SEQ ID NO.: 629 YYCSSYGG SEQ ID NO.: 630 YYCSSYGGT SEQ ID NO.: 631 YYCSSYGGTN SEQ ID NO.: 632 YYCSSYGGTNN SEQ ID NO.: 633 YYCSSYGGTNNL SEQ ID NO.: 634 YYCSSYGGTNNLL SEQ ID NO.: 635 YYCSSYGGTNNLLF SEQ ID NO.: 636 YYCSSYGGTNNLLFG SEQ ID NO.: 637 YYCSSYGGTNNLLFGG SEQ ID NO.: 638 YYCSSYGGTNNLLFGGG SEQ ID NO.: 639 YYCSSYGGTNNLLFGGGT Heavy chain variable domain (SEQ ID NO: 640) QMQLMQSGAEVKKPGASVTVSCKASGDTFSDYRIHWVRQAPGQGLEWMGRMNPKS GDTNFAQKFQGRVTMTRDMSINTAYMTLSGLTFDDTALYYCASLLIVGGFDPLDDFE VWGQGTMVTISS Light chain variable domain (SEQ ID NO: 641) QSALTQPPSASGSPGQSVTISCSGTSSDVGGYNFVSWYQHHPGKAPKILIYEVTKRPS GVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYGGTNNLLFGGGTKLTVL Heavy chain FR1 region (SEQ ID NO:642) SEQ ID NO:642 QMQLMQSGAEVKKPGASVTVSCKASGDTFS Heavy chain FR2 region (SEQ ID NO:643) SEQ ID NO:643 WVRQAPGQGLEWMG Heavy chain FR3 region (SEQ ID NO:644) SEQ ID NO:644 RVTMTRDMSINTAYMTLSGLTFDDTALYYCAS Heavy chain FR4 region (SEQ ID NO:645) SEQ ID NO:645 WGQGTMVTISS Light chain FR1 region (SEQ ID NO:646) SEQ ID NO:646 QSALTQPPSASGSPGQSVTISC Light chain FR2 region (SEQ ID NO:647) SEQ ID NO:647 WYQHHPGKAPKILIY Light chain FR3 region (SEQ ID NO:648) SEQ ID NO:648 GVPDRFSGSKSGNTASLTVSGLQAEDEADYYC

[0003] Light chain FR4 region (SEQ ID NO:649) SEQ ID NO:649 FGGGTKLTVL Heavy chain CDR1 region (SEQ ID NO:650) SEQ ID NO.: 650 YFYLH Heavy chain CDR2 region (SEQ ID NO: 651) SEQ ID NO.: 651 IINPRGDGTRYAQKFQG Heavy chain CDR3 region (SEQ ID NO: 652) SEQ ID NO.: 652 GADHGAFDI Light chain CDR1 region (SEQ ID NO: 653) SEQ ID NO.: 653 RASQSVRRNYFA Light chain CDR2 region (SEQ ID NO: 654) SEQ ID NO.: 654 DASTRAT Light chain CDR3 region (SEQ ID NO: 655) SEQ ID NO.: 655 QQYDSSPPMYI Heavy chain CDR1 region (SEQ ID NO: 656) SEQ ID NO.: 656 GYAMH Heavy chain CDR2 region (SEQ ID NO: 657) SEQ ID NO.: 657 VISRDARNKYYADSVKG Heavy chain CDR3 region (SEQ ID NO: 658) SEQ ID NO.: 658 LIIPGITEPGSPDALDI Light chain CDR1 region (SEQ ID NO: 659) SEQ ID NO.: 659 RASQDISKWLA Light chain CDR2 region (SEQ ID NO: 660) SEQ ID NO.: 660 AASSLQS Light chain CDR3 region (SEQ ID NO: 661) SEQ ID NO.: 661 QQASSFPWSIT Heavy chain CDR1 region (SEQ ID NO: 662) SEQ ID NO.: 662 SHYMH Heavy chain CDR2 region (SEQ ID NO: 663) SEQ ID NO.: 663 IINPSGSGTAYGQKFQG Heavy chain CDR3 region (SEQ ID NO: 664) SEQ ID NO.: 664 GSGGLFAY Light chain CDR1 region (SEQ ID NO: 665) SEQ ID NO.: 665 RASQIVRSNYLA Light chain CDR2 region (SEQ ID NO: 666) SEQ ID NO.: 666 GASSRAT Light chain CDR3 region (SEQ ID NO: 667) SEQ ID NO.: 667 LQYDSSPPTYI Heavy chain CDR1 region (SEQ ID NO: 668) SEQ ID NO.: 668 SYYMH Heavy chain CDR2 region (SEQ ID NO: 669) SEQ ID NO.: 669 LITPSGDDTYYAQRFQG Heavy chain CDR3 region (SEQ ID NO: 670) SEQ ID NO.: 670 MSRAGGFDV Light chain CDR1 region (SEQ ID NO: 671) SEQ ID NO.: 671 RASQSITGRYLA Light chain CDR2 region (SEQ ID NO: 672) SEQ ID NO.: 672 GESSRVT Light chain CDR3 region (SEQ ID NO: 673) SEQ ID NO.: 673 QHFASSPPTYT Heavy chain (SEQ ID NO: 674) SEQ ID NO.: 674 QEQLVQSGAEVKKPGASVKVSCKSSGFTFSYFYLHWVRQAPGQGLEWMGIIN PRGDGTRYAQKFQGRVTMTRDASTGTLYMELRSLRSEDTAVYYCARGADHGAFDIW GQGTMVTVSSASVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR GECDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVK FNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALP APIEKTISKAKGQPREPQVCTLPPSRDELTKNQVSLSCAVKGFYPSDIAVEWESNGQP ENNYKTTPPVLDSDGSFFLVSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSL SPGK Light chain (SEQ ID NO: 675) SEQ ID NO.: 675 EIVLTQSPGTLSLSPGERATLSCRASQSVRRNYFAWYQQKRGQAPRLLIYDASTRATG IPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYDSSPPMYIFGQGTKLEIKSSASTKG PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC Heavy chain of arm (SEQ ID NO: 676) SEQ ID NO.: 676 QMQLMQSGAEVKKPGASVTVSCKASGDTFSDYRIHWVRQAPGQGLEWMGRMNPKS GDTNFAQKFQGRVTMTRDMSINTAYMTLSGLTFDDTALYYCASLLIVGGFDPLDDFE VWGQGTMVTISSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNW YVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPCRDELTKNQVSLWCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG K Light chain of arm (SEQ ID NO: 677) SEQ ID NO.: 677 QSALTQPPSASGSPGQSVTISCSGTSSDVGGYNFVSWYQHHPGKAPKILIYEVTKRPS GVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYGGTNNLLFGGGTKLTVLGQPKA APSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSN NKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS Heavy chain arm (SEQ ID NO: 678) SEQ ID NO.: 678 QEQLVQSGAEVKKPGASVKVSCKSSGFTFSYFYLHWVRQAPGQGLEWMGIINPRGD GTRYAQKFQGRVTMTRDASTGTLYMELRSLRSEDTAVYYCARGADHGAFDIWGQGT MVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTC PPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVE VHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKA KGQPREPQVYTLPPCRDELTKNQVSLWCLVKGFYPSDIAVEWESNGQPENNYKTTP PVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Light chain arm (SEQ ID NO: 679) SEQ ID NO.: 679 EIVLTQSPGTLSLSPGERATLSCRASQSVRRNYFAWYQQKRGQAPRLLIYDASTRATG IPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYDSSPPMYIFGQGTKLEIKRTVAAPS VFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDS TYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Heavy chain of arm (SEQ ID NO: 680) SEQ ID NO.: 680 QMQLMQSGAEVKKPGASVTVSCKASGDTFSDYRIHWVRQAPGQGLEWMGRMNPKS GDTNFAQKFQGRVTMTRDMSINTAYMTLSGLTFDDTALYYCASLLIVGGFDPLDDFE VWGQGTMVTISGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADS SPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPT ECSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKF NWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPA PIEKTISKAKGQPREPQVCTLPPSRDELTKNQVSLSCAVKGFYPSDIAVEWESNGQPE NNYKTTPPVLDSDGSFFLVSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLS PGK Light chain of arm (SEQ ID NO: 681) SEQ ID NO.: 681 QSALTQPPSASGSPGQSVTISCSGTSSDVGGYNFVSWYQHHPGKAPKILIYEVTKRPS GVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYGGTNNLLFGGGTKLTVLSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC Heavy chain of arm (SEQ ID NO: 682) SEQ ID NO.: 682 QSALTQPPSASGSPGQSVTISCSGTSSDVGGYNFVSWYQHHPGKAPKILIYEVTKRPS GVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYGGTNNLLFGGGTKLTVLGQPKA APSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSN NKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSDKTHTCPPCPAPEL LGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTK PREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VCTLPPSRDELTKNQVSLSCAVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLVSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Light chain o (SEQ ID NO: 683) SEQ ID NO.: 683 QMQLMQSGAEVKKPGASVTVSCKASGDTFSDYRIHWVRQAPGQGLEWMGRMNPKS GDTNFAQKFQGRVTMTRDMSINTAYMTLSGLTFDDTALYYCASLLIVGGFDPLDDFE VWGQGTMVTISSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC Heavy chain variable domain arm (SEQ ID NO: 684) SEQ ID NO.: 684 QVQLVESGGGVVQPGRSLRLSCAASGLTFSGYAMHWVRQAPGKGLEWVAVISRDAR NKYYADSVKGRFTISRDNSKKTVYLEMNSLRVEDTAVYYCAILIIPGITEPGSPDALDI WGQGTMVSVSS Light chain variable domain (SEQ ID NO: 685) SEQ ID NO.: 685 DIQMTQSPSSMSASVGDRVTITCRASQDISKWLAWYQQRPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQASSFPWSITFGQGTRLEIR Heavy chain variable domain arm (SEQ ID NO: 686) SEQ ID NO.: 686 QEQLVQSGAEVKKPGASVKVSCKSSGFTFSYFYLHWVRQAPGQGLEWMGIINPRGD GTRYAQKFQGRVTMTRDASTGTLYMELRSLRSEDTAVYYCARGADHGAFDIWGQGT MVTVSS Light chain variable domain (SEQ ID NO: 687) SEQ ID NO.: 687 EIVLTQSPGTLSLSPGERATLSCRASQSVRRNYFAWYQQKRGQAPRLLIYDASTRATG IPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYDSSPPMYIFGQGTKLEIK Heavy chain variable domain arm (SEQ ID NO: 688) SEQ ID NO.: 688 QVQLVQSGAEVKKPAASVKVSCKASGDTFSSHYMHWVRQAPGQGPEWMGIINPSGS GTAYGQKFQGRLTMTRDTSTSTVYMELSSLTSDDTAVYYCGGGSGGLFAYWGQGTL VTVSS Light chain variable domain (SEQ ID NO: 689) SEQ ID NO.: 689 EIVLTQSPGTLSLSPGERATLSCRASQIVRSNYLAWYQQKPGQAPRLLIYGASSRATGT PDRFSGGGSGTDFTLTINRLEPEDFAVYYCLQYDSSPPTYIFGQGTKLEIK EXAMPLES Example 1: Antibody according to the invention (Intraperitoneal) The aim of this study was to assess the pre-exposure efficacy of a monoclonal antibody according to the invention, having a heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, following systemic intraperitoneal administration in a SARS-CoV-2 Delta K18 hACE2 Tg mouse model. Animals (n=10 per group) were treated with an intraperitoneal dose range of the test monoclonal antibody (10 to 0.2 mg / kg) or PBS control as vehicle at study day -1. At study day 0 animals were challenged with 103.5TCID50 of SARS-CoV-2 Delta variant. Materials and Methods The monoclonal antibody according to the invention, which is buffered in phosphate- buffered saline PBS was diluted with (PBS) to the final concentrations for administration (10 to 0.2mg / kg in 200 µL), thereby preparing a monoclonal antibody dilution. The monoclonal antibody dilution was made up at various concentrations so that 200 uL administrations to the mean weight per cage of the dosing group at day -5 resulted in monoclonal antibody doses ranging from 10 mg / kg, 5 mg / kg, 1.7 mg / kg, 0.5 mg / kg to 0.2 mg / kg. The antibody was stored at -85°C ± 10°C and dilutions were stored at 4°C until usage and the temperature of the storage unit was monitored. The virus strain tested was SARS-CoV-2 Delta variant (Aus / VIC / 18440 / 2021 (B.1.617.2)., which has been passed three times through Vero-hSLAM cells. Animals The animal species used was the SARS-CoV-2 Delta K18 hACE2 Tg (B6.Cg-Tg(K18- ACE2)2Prlmn / JArc; Jax™ Stock No.: 034860) mouse model, at a weight of c. 16-21 g on day -5.60 mice were used at the age of 8-9 weeks on the day of test article administration and were exclusively female. Ten animals were allocated to 6 treatment groups based on day -5 weight to create groups with similar mean weight. All mice were housed in individually ventilated cages (IVCs), with corn cob bedding, tissues or shredded paper as nesting material, a wooden chew block, accessible food pellets and acidic water for animal nourishment and red plastic tunnels. Each cage system holds 3 to 5 mice per cage. All mice were transferred to fresh cages every 14 days. Food and water were inspected daily and topped up as needed. Each animal was weighed daily beginning at the day of infection (Day 0). Study design The dose level of monoclonal antibody applied in the current example was based on the maximal dosing possible for the material stock concentration (4 mg / ml) and based on literature and previous experience with an anti-S2 antibody (CV3-25) showing protection IP at doses ≥0.5mg / kg. A total number of 60 mice, 8-9 weeks of age at the time of test article administration, were allocated to 6 experimental groups according to Table 1 (see below). Mice were given a period of >3 days for acclimatization. Table 1: Intraperitoneal experimental detail Female SARS-CoV-2 Delta K18 hACE2 mice were treated via the intraperitoneal route of administration with the antibody at a dose between 10 mg / kg and 0.2 mg / kg based upon average weight per cage. On Day 0, all mice were challenged with a lethal dose (103.5TCID50) of the SARS-CoV-2 Delta variant and observed for weight loss and mortality until the end of the study at day 14. Antibody administration The test antibody was stored at -80°C upon arrival. The appropriate dose, according to the treatment schedule (Table1), was formulated assuming the average weight per cage. Prior to dosing, the material was drawn into a 1mL syringe with a 26G needle and then administered to each mouse. Mice in the treatment group received the indicated dose by intraperitoneal administration of 200 μL of antibody solution into the intraperitoneal cavity, mice were scruffed and held inverted at a -45 deg angle for administration (200 μL per mouse). Mice in the vehicle group receiving PBS were anaesthetized with isoflurane (4% v / v with 2L / min O2) for two minutes. The mice were then scruffed and held at a +45 deg angle.50uL of compound or vehicle control was then slowly administered to the nares of each mouse (25 μL each nare). The mice were held for an additional 5-10 seconds to ensure compound delivery to the lower respiratory tract before being put back into the home box. Virus administration The virus material was stored at -80°C and was defrosted prior to administration, at a titer of 106.3TCID50 / mL. Once defrosted, the material was diluted in sterile PBS corresponding to approximately 103.5TCID50 / 50 μL). As required, the animals were anesthetized by isoflurane (4% v / v with 2L / min O2) and each animal received approximately 50 μL (25 μL in each nare) of virus corresponding with approximately 103.5TCID50 by intranasal inoculation. Unused material was frozen at -20 to -80°C for back titration. Laboratory analysis Inoculum was back titrated and the actual dose of the virus administered was verified by titrating replicate samples on Vero cells. Terminal investigations At the end of the study, on day 14, mice were euthanized by cervical dislocation. Gross necropsy was not performed. Data analysis and statistical methods Survival proportions at day 14, survival times and change in bodyweight (Area Under the Curve) were compared to the control group using Fisher’s exact test, log-rank and Welch's t-test, respectively. All groups were compared to the vehicle (PBS solution) control group. P-values were adjusted according to Bonferroni (for two comparisons to vehicle) followed by a stepwise approach (starting with the highest antibody dose conditionally testing a lower dose if the previous step was statistically significant). Statistical analysis was performed using R and statistical significance was set at α = 0.05. Survival Prophylactic treatment with ≥ 0.5 mg / kg test antibody provided a statistically significant increase in survivalcompared to vehicle (See Figure 1). The animals that were treated with with 0.5 mg / kg had a 60% survival rate, with 1.7 and 5 mg / kg test antibody a 100% survival rate and with 10 mg / kg a rate of 90%. Whereas the control group showed 0% survival at day 7 with a median survival time of 6 days. Prophylactic treatment with ≥ 0.2 mg / kg test antibody resulted in a significant improvement in survival time. Body weight Change in bodyweight was analyzed using an Area Under the Curve (AUC) analysis in which the last observed body weight was carried forward if a mouse died / was euthanized during the study. The weight per mouse at day 0 was used as baseline and weight change was determined relative to baseline and the net AUC was defined as the summation of the area above and below the baseline using the percentage change per day. Prophylactic treatment with ≥ 0.5 mg / kg test antibody resulted in a significant reduction in weight loss compared to the control group. Conclusion In this lethal SARS-CoV-2 Delta K18 hACE2 Tg mouse model, the prophylactic intraperitoneal administration of ≥ 0.5 mg / kg test antibody provides significant improvement in survival compared to vehicle and a reduction in weight loss whereas all the animals in the control group died. Example 2: Antibody according to the invention (Intranasal) The aim of this study was to assess the pre-exposure efficacy of the monoclonal antibody according to the invention following systemic intranasal administration in a SARS-CoV- 2 Delta K18 hACE2 Tg mouse model. Animals (n=10 per group) were treated with an intranasal dose range of the test monoclonal antibody (10 to 0.2 mg / kg) or PBS control at study day -1. At study day 0, animals were challenged with 103.5TCID50 of SARS-CoV-2 Delta variant. Materials and Methods The monoclonal antibody according to the invention is buffered in PBS was diluted with PBS to the final concentrations for administration (10 to 0.2 mg / kg in 50µL) The monoclonal antibody dilution was made up at various concentrations so that 50 uL administrations to the mean weight per cage of the dosing group resulted in antibody doses ranging from 10 mg / kg, 5 mg / kg, 1.7 mg / kg, 0.5 mg / kg to 0.2 mg / kg. The antibody was stored at -85°C ± 10°C and dilutions were stored at 4°C until usage and the temperature of the storage unit was monitored. The virus strain tested was SARS-CoV-2 Delta variant (Aus / VIC / 18440 / 2021 (B.1.617.2)., which has been passed three times through Vero-hSLAM cells. Animals The animal species used was the SARS-CoV-2 Delta K18 hACE2 Tg mouse model, at a weight of c.16-22 g on the day of test article administration.60 mice were used at the age of 8-9 weeks on the day of test article administration and were exclusively female. Ten animals were allocated to 6 treatment groups based on Day -5 weights to create groups with similar weights. All mice were housed in individually ventilated cages (IVCs), with corn cob bedding, tissues or shredded paper as nesting material, a wooden chew block, accessible food pellets and acidic water for animal nourishment and red plastic tunnels. Each cage system holds 3 to 5 mice per cage. All mice were transferred to fresh cages every 14 days. Food and water were inspected daily and topped up as needed. Study design The dose level of monoclonal antibody applied in the current example was based on the maximal dosing possible for the material stock concentration (4 mg / ml) and based on literature and previous experience with an anti-S2 antibody (CV3-25) showing protection IN at doses ≥1.7 mg / kg. A total number of 60 mice, 8-9 weeks of age at the test article dosing time, were transported to the animal Facility and allocated to 6 experimental groups according to Table 2 (see below). Mice were given a period of >3 days for acclimatization. Table 2: Intranasal experimental detail Female SARS-CoV-2 Delta K18 hACE2 mice were treated via the intranasal route of administration with the antibody at a dose between 10 mg / kg and 0.2 mg / kg based upon average weight per cage. On Day 0, all mice were challenged with a lethal dose (103.5TCID50) of the SARS-CoV-2 Delta variant and observed for survival and weight loss until the end of the study at day 14. Antibody administration The test antibody was stored at -80°C upon arrival. The appropriate dose, according to the treatment schedule (Table 2), was formulated based upon average weight per cage. Just prior to dosing, the material was drawn into a 1mL syringe with a 26G needle, and then administered to each mouse. Mice were anaesthetized with isoflurane (4% v / v with 2L / min O2) for two minutes. The mice were then scruffed and held at a +45 deg angle. 50uL of compound or vehicle control was then slowly administered to the nares of each mouse (25 μL each nare). The mice were held for an additional 5-10 seconds to ensure compound delivery to the lower respiratory tract before being put back into the home box. Virus administration The virus material was stored at -80°C and was defrosted prior to administration. Once defrosted, the material was diluted in cold PBS corresponding to approximately 103.5TCID50 / 50 μL. As required, the animals were anesthetized by isoflurane (4% v / v with 2L / min O2) and each animal received approximately 50 μL (25 μL each nare) of virus corresponding with approximately 103.5TCID50 by intranasal inoculation. Unused material was frozen at -20 to -80°C for back titration. Laboratory analysis Inoculum was back titrated and the dose of the virus administered was verified by titrating replicate samples on Vero cells. Terminal investigations At the end of the study, on day 14, mice were euthanized by cervical dislocation. Gross necropsy was not performed. Data analysis and statistical methods Survival proportions at day 14, survival times and change in bodyweight (Area Under the Curve) were compared to the corresponding control group using Fisher’s exact test, log- rank and Welch's t-test, respectively. All groups were compared to the vehicle (PBS solution) control group. P-values were adjusted according to Bonferroni (for two comparisons to vehicle) followed by a stepwise approach (starting with the highest antibody dose conditionally testing a lower dose if the previous step was statistically significant). Statistical analysis was performed using R and statistical significance was set at α = 0.05. Survival Prophylactic treatment with >0.5 mg / kg test antibody provided a statistically significant increase in survival compared to vehicle control (See Figure 2). Whereas the control group showed 0% survival at Day 7 with a median survival time of 6 days. Prophylactic treatment with >0.2 mg / kg test antibody resulted in a significant improvement in survival time. Body weight Change in bodyweight was analyzed using an Area Under the Curve (AUC) analysis in which the last observed body weight was carried forward if a mouse died / was euthanized during the study. The weight per mouse at day 0 was used as baseline and weight change was determined relative to baseline and the net AUC was defined as the summation of the area above and below the baseline using the percentage change per day. Prophylactic treatment with >0.2 mg / kg test antibody resulted in a significant reduction in weight loss compared to the control group. Conclusion In this lethal SARS-CoV-2 Delta K18 hACE2 Tg mouse model, the prophylactic intranasal administration of ≥0.5 mg / kg test antibody provides significant improvement in survival and a reduction in weight loss compared to vehicle. In contrast, all the animals in the control group had died by day 7. Example 3: Antibody according to the invention The aim of this study is to assess the pre- and post- exposure efficacy of a monoclonal antibody according to the invention, having a heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584, following intranasal administration in a NHP model in which each subject is pre-screened for the absence of serum antibodies against SARS-CoV-2 viruses. NHP subjects are treated with an intranasal dose of the composition comprising the antibody described above. The flat dose, or nominal dose, of the antibody administered to each NHP subject is between 0.01 mg and 10 mg (e.g. between0.01 to 2.0 mg (“Low Dose”) or between 2.0 to 10 mg (“High Dose”)) or Control (e.g. vehicle only) at study day -1. Materials and Methods The monoclonal antibody according to the invention is provided in a sodium acetate buffer (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5) and is diluted to the final concentration for administration ranging from 0.01 mg to 2.0 mg or 2.0 to 10 mg nominal dose, administered as 50 µL to 500 µL per nare. The NHP subjects allocated to the Control Group (Sodium acetate buffer) are administered with vehicle (e.g. 20 mM Sodium Acetate, 75 mM Sodium Chloride, 5% sucrose, pH 5.5), administered as 50 µL to 500 µL per nare. All NHPs receive intranasal challenge with SARS-CoV-2 at day 0. Samples are taken during the study, sample types include nasal sampling (e.g. nasal swabs, wash or scrapes), serum and / or bronchoalveolar lavage (BAL) samples. Sampling period includes study duration, in a time frame between day -1 to the end of the study (7 to 21 days follow-up period). Samples are analyzed as required for viral quantification (by RT-PCR and / or TCID50) and / or antibody titers and neutralization titers by ELISA, HPLC or similar method and in-vitro neutralization assay (e.g. Pseudovirion neutralization). Animals The NHP subjects are used at a weight of between 3 to 12 kg (e.g. 5 kg per animal) on commencement of the study. Between 4 and 12 animals are allocated to each treatment group. Study design The dose level of the monoclonal antibody applied in the current example is based on the maximal dosing and a lower dose based upon allometric calculations obtained from murine studies. Table 3: Intranasal experimental detail per antibody The NHP subjects receive intranasal administrations with compositions comprising the antibody at a dose between 0.01 mg to 2.0 mg or 2.0 mg to 10 mg (Nominal Dose). On Day 0, all NHP subjects are challenged with a dose of the SARS-CoV-2 and observed for clinical manifestations (e.g. weight loss and / or temperature) and virology measurements until the end of the study (e.g. Day 7 to 21). Antibody administration The test antibody or vehicle only is administered to each nare (e.g. pipette or spray) according to the treatment schedule (Table 3), using volumes of between 50 µL to 500 µL per nare. Virus administration The virus material is defrosted prior to administration. Once defrosted, the material is diluted and each animal receives between 50 μL to 500 μL of virus solution per nare. The NHP subjects are infected with between 102and 108TCID50of SARS-CoV-2 (e.g. 105TCID50of SARS-CoV-2). Data analysis and statistical methods Clinical manifestations (e.g. body weight loss and temperature) and virological measurements are used for comparisons between treatment and Control Group. Results – Clinical Manifestations Prophylactic treatment with the Low Dose and High Dose antibody administration provides reduction in clinical manifestation measurements, compared to the Control Group. Results – Virological Measurements Prophylactic treatment with the Low Dose and High Dose antibody administration provides reduction in virological measurements, compared to the Control Group. All Control Group NHPs show viral loads in samples after SARS-CoV-2 challenge. Conclusion In this SARS-CoV-2 NHP model, the prophylactic intranasal administration of 2.0 to 10 mg (High Dose) and 0.01 to 2.0 mg (Low Dose) of the test antibody according to the invention provides a reduction in virological measurements and / or a reduction in clinical manifestations as compared with Control Group NHPs. Example 4: Composition comprising an antibody according to the invention The aim of this study is to assess the pre- and post- exposure efficacy of a composition comprising a first monoclonal antibody according to the invention, having a heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584 (“First Antibody”), and a second monoclonal antibody according to the invention, having a heavy chain CDR1 as SEQ ID NO: 656, heavy chain CDR2 as SEQ ID NO: 657, heavy chain CDR3 as SEQ ID NO: 658, a light chain CDR1 as SEQ ID NO: 659, a light chain CDR2 as SEQ ID NO: 660, and a light chain CDR3 as SEQ ID NO: 661 (“Second Antibody”), following intranasal administration in a NHP model in which each subject is pre-screened for the absence of serum antibodies against SARS-CoV-2 viruses. NHP subjects are treated with an intranasal dose of the composition comprising the antibodies described above (single antibodies or combinations of both antibodies). The flat dose, or nominal dose, of the antibodies administered to each NHP subject is between 0.003 mg and 5 mg or Control (e.g. vehicle only) at study day -1 Materials and Methods The monoclonal antibody according to the invention is provided in a sodium acetate buffer (e.g. 20 mM Sodium Acetate, 75 mM Sodium Chloride, 5% sucrose, pH 5.5) and is diluted to the final concentration for administration ranging from 0.003 mg and 5 mg nominal dose, administered as 50 µL to 500 µL per nare. The NHP subjects allocated to the Control Group (Sodium acetate buffer) are administered with vehicle (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5), administered as 50 µL to 500 µL per nare. All NHPs receive intranasal challenge with SARS-CoV-2 at day 0. Samples are taken during the study, sample types include nasal sampling (e.g. nasal swabs, wash or scrapes), serum and / or bronchoalveolar lavage (BAL) samples. Sampling period includes study duration, in a time frame between day -1 to the end of the study (7 to 21 days follow-up period). Samples are analyzed as required for viral quantification (by RT-PCR and / or TCID50) and / or antibody titers and neutralization titers by ELISA, HPLC or similar methods. Animals The NHP subjects are used at a weight of between 3 to 12 kg (e.g. 5 kg per animal) on commencement of the study. Between 4 and 12 animals are allocated to each treatment group. Study design The dose level of the monoclonal antibody and the combination applied in the current example is based on the maximal dosing and based upon allometric calculations obtained from murine studies. Table 4: Intranasal experimental detail The NHP subjects receive intranasal administrations with compositions comprising either single antibody nominal doses of between 0.003 - 5 mg (Treatment Groups 1 or 2). Different NHP subjects receive intranasal administrations with compositions comprising the First and Second Antibody at nominal doses between 0.003 - 5 mg (Treatment Group 3). On Day 0, all NHP subjects are challenged with a dose of the SARS-CoV-2 and observed for clinical manifestations (e.g. weight loss and / or temperature) and virology measurements until the end of the study (e.g. Day 7 to 21). Antibody administration The antibody compositions (Treatment Groups 1 to 3) or vehicle only are administered to each nare (e.g. pipette or spray) according to the treatment schedule (Table 4), using volumes of between 50 µL to 500 µL per nare. Virus administration The virus material is defrosted prior to administration. Once defrosted, the material is diluted and each animal receives between 50 μL to 500 μL of virus solution per nare. The NHP subjects are infected with between 102and 108TCID50of SARS-CoV-2 (e.g. 105TCID50of SARS-CoV-2). Data analysis and statistical methods Clinical manifestations (e.g. body weight loss and temperature) and virological measurements are used for comparisons between treatments (e.g. Treatment Groups 1 to 3) and Control Group and / or comparison within treatment groups (e.g. Treatment Group 1 against Treatment Group 3). Results – Clinical Manifestations Prophylactic treatment with treatments (as indicated in Table 4) provides reduction in clinical manifestation measurements, compared to the Control Group or compared within treatment groups. Results – Virological Measurements Prophylactic treatment with treatments (as indicated in Table 4) provides reduction in virological measurements, compared to the Control Group or compared within treatment groups. Conclusion In this SARS-CoV-2 NHP model, the prophylactic intranasal administration of treatments (as indicated in Table 4) according to the invention provides a reduction in clinical manifestations and / or a reduction in virological measurements, as compared with control group NHPs and within treatments. Example 5: Bi-specific antibody according to the invention The aim of this intranasal murine study is to assess the pre- and post- exposure efficacy of a bispecific monoclonal antibody in comparison with the parental antibodies, according to the invention, having a first Fab capable of binding to the stem helix of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 013, 170, 266, 386, 439 or 584; wherein the second Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 656, 657, 658, 659, 660 to 661. Animals are treated with an intranasal nominal dose (0.001 mg / kg to 15 mg / kg) comprising either Parental mAb 1, or Parental mAb 2, or the bispecific antibody described above, or vehicle control at study day -1. Materials and Methods The monoclonal parental and bispecific antibodies according to the invention is provided in a sodium acetate buffer (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5) and is diluted to the final concentration for administration ranging from 0.001 mg / kg to 15 mg / kg, administered as 25 µL to 50 µL per nare. The mice allocated to the control group (Sodium acetate buffer) are administered with vehicle (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5), administered as 25 µL to 50 µL per nare. All mice receive intranasal challenge with SARS-CoV-2 Delta at day 0. Animals The SARS-CoV-2 Delta K18 hACE2 Tg mice are used at a weight of c.15g to 22g (e.g. 20 g per animal) on commencement of the study. Between 6 and 10 animals are allocated to each treatment group. Study design The dose level of the monoclonal and bispecific antibodies applied in the current example is based on the maximal dosing and based upon previous results from efficacy studies in mice with the parental antibodies alone. From the maximal dose of ≤15 mg / kg, a 3- or 4- fold dilution curve for each the parental or bispecific antibody is applied.

[0004] Table 5: Intranasal experimental detail per antibody The mice are treated via the intranasal route of administration with compositions comprising either parental antibodies or the bispecific antibody at dose ranges between 0.001 and 15 mg / kg. On Day 0, all mice are challenged with a dose of the SARS-CoV-2 and observed for survival and body weight until the end of the study (e.g. Day 10-15). Antibody administration The parental monoclonal antibodies or bispecific antibody or vehicle only is administered to each nare (e.g. pipette or spray) according to the treatment schedule (Table 5), using volumes of between 25 µL to 50 µL per nare. Virus administration The virus material is defrosted prior to administration. Once defrosted, the material is diluted and each animal received between 25 μL to 50 μL of virus per nare. The mice are infected with between 102and 108TCID50of SARS-CoV-2 (e.g. 103.5TCID50of SARS-CoV- 2). Laboratory analysis Inoculum is returned to the lab and the dose of the virus administered is verified by titrating replicate samples on Vero cells. Clinical monitoring General health observations are performed on each animal from the day of arrival until the end of the study at least once daily (during normal servicing procedures). Each animal is weighed daily beginning one day prior to infection (day -1). Data analysis and statistical methods Survival proportions and survival times and change in bodyweight (Area Under the Curve) are compared to the corresponding control group using Fisher’s exact test, log- rank and Welch's t-test, respectively. All groups are compared to the vehicle control group. P values are adjusted according to Bonferroni (for three comparisons to vehicle) followed by a stepwise approach within antibody (starting with the highest dose and conditionally testing a lower dose if the previous step was statistically significant). Combination index Survival dose response curves are fitted for each of the treatments (Parental mAb 1, Parental mAb 2 and Bispecific) and the ED50is estimated. The efficacy of the bispecific antibody is then compared to the parental antibodies by calculation of the combination index. Survival Prophylactic treatment with Parental mAb 1, Parental mAb 2 or bispecific antibody (as indicated in Table 5) compared to the control group provides statistically significant protection against mortality and a significant improvement in survival time compared to the control group. Body weight Change in bodyweight is analyzed using an Area Under the Curve (AUC) analysis in which the last observed body weight is carried forward if a mouse died / is euthanized during the study. The weight per mouse at day 0 is used as baseline and weight change is determined relative to baseline with the net AUC defined as the summation of the area above and below the baseline using the percentage change per day. Prophylactic treatment with the parental or bispecific antibodies (as indicated in Table 5) provides a statistically significant reduction in weight loss, compared to the control group. Conclusion In this SARS-CoV-2 Delta mouse model, the prophylactic intranasal administration of a bispecific antibody (as indicated in Table 5) according to the invention provides significant improvement in survival and a reduction in body weight loss compared with Control Group. The outcome of the combination index is suggestive of at least a comparable, an additive or potentially synergistic effect for the bispecific compared to the parental antibodies. Example 5a: Bi-specific antibody according to the invention The aim of this intranasal murine study was to assess the pre- and post- exposure efficacy of a bispecific monoclonal antibody in comparison with the parental antibodies, according to the invention, having a first Fab capable of binding to the stem helix of SARS-CoV-2 and a second Fab capable of binding to the fusion peptide of SARS-CoV-2. The first parental antibody (“Parental mAb 1”) has the following CDRs as described in SEQ ID Numbers: 013, 170, 266, 386, 439, and 584. The second parental antibody (“Parental mAb 2”) has the following CDRs as described in SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. The bi-specific antibody according to the invention has a first Fab that comprises a sequence comprising any one or more of SEQ ID Numbers: 013, 170, 266, 386, 439, and 584; the second Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. Animals (n= 8 per group) were treated with an intranasal dose comprising either 0.007 mg / kg to 1.7 mg / kg (Parental mAb 1 or Parental mAb 2), or 0.002 mg / kg to 10 mg / kg (bispecific antibody) described above, or vehicle control at study Day -1. Materials and Methods The monoclonal parental antibodies and the bispecific antibody according to the invention were provided in a sodium acetate buffer (20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5) and the bispecific antibody according to the invention was provided in phosphate buffered saline (PBS) and all antibodies were diluted to the final concentration for administration ranging from either 0.007 mg / kg to 1.7 mg / kg (Parental mAb 1 or Parental mAb 2), or 0.002 mg / kg to 10 mg / kg (bispecific antibody), administered as 25 µL per nare. The mice allocated to the control group were administered with vehicle (phosphate buffered saline, PBS), administered as 25 µL per nare. The virus strain tested was SARS-CoV-2 Delta variant (Aus / VIC / 18440 / 2021 (B.1.617.2)., which has been passed three times through Vero-hSLAM cells. Animals The animal species used was the SARS-CoV-2 Delta K18 hACE2 Tg (B6.Cg-Tg(K18- ACE2)2Prlmn / JArc; Jax™ Stock No.: 034860) mouse model, at a weight of c. 13.6- 22.6 g at Day 0. A total of 144 mice were used at the age of 7-11 weeks and were exclusively female. Eight animals were allocated to 17 treatment groups to create groups with similar mean weight. Eight mice we allocated to a vehicle control group. All mice were housed in individually ventilated cages (IVCs), with corn cob bedding, tissues or shredded paper as nesting material, a wooden chew block, accessible food pellets and acidic water for animal nourishment and red plastic tunnels. Each cage system holds 3 to 5 mice per cage. All mice were transferred to fresh cages every 14 days. Food and water were inspected daily and topped up as needed. Each animal was weighed daily beginning at the day of infection (Day 0). Study design The dose level of the parental antibodies and a combination thereof applied in the current example was based on previous experience with these antibodies intranasally showing protection IN at doses ≥ 0.5 mg / kg (Parental mAb 1) and ≥ 0.2 mg / kg (Parental mAb 2). The potency of the bispecific antibody of the two parental antibodies is expected to be similar, and one dose step up and down from the dose range for the parental antibodies was included for the bispecific antibody. A total number of 144 mice, 7-11 weeks of age, were allocated to 18 experimental groups according to Table 6 (see below). Mice were given a period of > 3 days for acclimatization. Table 6: Intranasal experimental detail for parental antibodies and bispecific antibody. The mice were treated via the intranasal route of administration with compositions comprising either parental antibodies or the bispecific antibody at dose ranges between 0.002 and 10 mg / kg. On Day 0, all mice were challenged with a dose of the SARS-CoV-2 and observed for survival and body weight until the end of the study (Day 14). Antibody administration The test antibody was stored at -80°C ± 10°C upon arrival. The appropriate dose, according to the treatment schedule (Table 6), was formulated based upon the average weight per cage Just prior to dosing, the material was drawn into a 1 mL syringe with a 26G needle, and then administered to each mouse. Mice were anaesthetized with isoflurane (4% v / v with 2 L / min O2) for two minutes. The mice were then scruffed and held at a +45 deg angle.50 µL of compound or vehicle control was then slowly administered to the nares of each mouse (25 µL each nare). The mice were held for an additional 5 to 10 seconds to ensure compound delivery to the lower respiratory tract before being put back into the home box. Virus administration The virus material was stored at -80°C ± 10°C and was defrosted prior to administration. Once defrosted, the material was diluted in cold PBS corresponding to approximately 103.5TCID50 / 50 μL. As required, the animals were anesthetized by isoflurane (4% v / v with 2 L / min O2) and each animal received approximately 50 μL (25 μL each nare) of virus corresponding with approximately 103.5TCID50by intranasal inoculation. Terminal investigations At the end of the study, on Day 14, mice were euthanized by cervical dislocation. Gross necropsy was not performed. Data analysis and statistical methods Survival proportions at Day 14, survival times and change in bodyweight (using the Area Under the Curve) were compared to the vehicle control group using a Fisher’s exact test, log-rank and Welch's t-test, respectively. P-values were adjusted according to Bonferroni for four comparisons against vehicle control, followed by a stepwise approach, within arm, starting with the highest dose and conditionally testing a lower dose if the previous dose was statistically significant. Survival proportions at Day 14 were used to estimate the survival dose response curve using Probit regression without assuming a parallel dose response curve for the treatments. The model was used to estimate the median effective dose and the ratio between the treatments was determined. Statistical analysis was performed using R and statistical significance was set at α = 0.05. Survival The vehicle control group showed 0% survival with a median survival time of 7 days. Prophylactic intranasal treatment with ≥ 0.11 mg / kg of either parental antibody intranasally provided a statistically significant increase in survival compared to control group (See Figure 5A and 5D). Prophylactic treatment with ≥ 0.16 mg / kg of the bispecific antibody provides statistically significant increase in survival compared to control group (See Figure 5G). Prophylactic intranasal treatment with ≥ 0.03 mg / kg of either parental antibody or ≥ 0.039 mg / kg of the bispecific antibody intranasally provides statistically significant increase in survival time compared to control group. Survival dose response curves The survival dose response curves were estimated using Probit regression without assuming a parallel dose response curve between treatments. The vehicle control group was included in the modelling at a dose of 0 mg / kg. The Probit regression model was used to estimate the antibody dose corresponding to 50% survival (ED50) (see Table 7 and Figure 5C, 5F and 5I). The intranasal median effective dose was lowest for the bispecific antibody, with 0.013 mg / kg and both parental antibodies were within a 4-fold ratio and no significant difference in ED50compared to the bispecific antibody was determined. Table 7: Estimated ED50’s (in mg / kg, rounded to 3 decimals). Body weight Change in bodyweight was analyzed using an Area Under the Curve (AUC) analysis in which the last observed body weight was carried forward if a mouse died / was euthanized during the study. The weight per mouse at Day 0 was used as baseline and weight change was determined relative to baseline with the net AUC defined as the summation of the were a above and below the baseline using the percentage change per day. Prophylactic intranasal treatment with ≥ 0.03 mg / kg of either parental antibody and ≥ 0.039 mg / kg of the bispecific antibody resulted in a significant reduction in weight loss compared to the control group (Figure 5B, 5E and 5H). Conclusion In this SARS-CoV-2 Delta mouse model, the prophylactic intranasal administration of a bispecific antibody (as indicated in Table 6) according to the invention at doses ≥ 0.16 mg / kg provides significant increases in survival and at doses ≥ 0.039 mg / kg a reduction in body weight loss compared with control group. Moreover, median effective doses of the bispecific antibody were not significantly different to the parental antibodies (Table 7).

[0005] Example 6: Composition comprising antibody combination according to the invention The aim of this intranasal murine study is to assess the pre- and post- exposure efficacy of a composition comprising a first antibody according to the invention capable of binding to the stem helix of SARS-CoV-2, and second antibody capable of binding to the fusion peptide of SARS-CoV-2. The first antibody (“First mAb”) having a heavy chain CDR1 as SEQ ID NO: 013, heavy chain CDR2 as SEQ ID NO: 170, heavy chain CDR3 as SEQ ID NO: 266, a light chain CDR1 as SEQ ID NO: 386, a light chain CDR2 as SEQ ID NO: 439, and a light chain CDR3 as SEQ ID NO: 584. The second antibody (“Second mAb”) having a heavy chain CDR1 as SEQ ID NO: 662, heavy chain CDR2 as SEQ ID NO: 663, heavy chain CDR3 as SEQ ID NO: 664, a light chain CDR1 as SEQ ID NO: 665, a light chain CDR2 as SEQ ID NO: 666, and a light chain CDR3 as SEQ ID NO: 667. Animals are treated with an intranasal dose (0.001 mg / kg to 15 mg / kg) of the comprising either First mAb, or Second mAb, or the composition comprising the first and second antibody described above, or vehicle control at study day -1. Materials and Methods The First mAb and Second mAb are provided in a sodium acetate buffer (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5) and is diluted to the final concentration for administration ranging from 0.001 to 15 mg / kg administered as 25 µL to 50 µL per nare. The mice allocated to the control group (Sodium acetate buffer) are administered with vehicle (e.g. 20mM Sodium Acetate, 75mM Sodium Chloride, 5% sucrose, pH 5.5), administered as 25 µL to 50 µL per nare. All mice receive intranasal challenge with SARS-CoV-2 Delta at day 0. Animals The SARS-CoV-2 Delta K18 hACE2 Tg mice are used at a weight of c.15g to 22g (e.g. 20 g per animal) on commencement of the study. Between 6 and 10 animals are allocated to each treatment group. Study design The dose level of the First mAb, or Second mAb, or the composition comprising the first and second antibody described above in the current example is based on the maximal dosing and based upon previous results from efficacy studies in mice with the parental antibodies alone. From the maximal dose of ≤15 mg / kg, a 3- or 4-fold dilution curve for each the parental or bispecific antibody is applied. Table 8: Intranasal experimental detail per antibody The mice are treated via the intranasal route of administration with compositions comprising either First or Second antibodies or the composition comprising the combination at dose ranges between 0.001 and 15 mg / kg. On Day 0, all mice are challenged with a dose of the SARS-CoV-2 and observed for survival and body weight until the end of the study (e.g. Day 10-15). Antibody administration The First or Second antibodies or the composition comprising the combination or vehicle only is administered to each nare (e.g. pipette or spray) according to the treatment schedule (Table 8), using volumes of between 25 µL to 50 µL per nare. Virus administration The virus material is defrosted prior to administration. Once defrosted, the material is diluted and each animal received between 25 μL to 50 μL of virus per nare. The mice are infected with between 102and 108TCID50of SARS-CoV-2 (e.g. 103.5TCID50of SARS-CoV- 2). Laboratory analysis Inoculum is returned to the lab and the dose of the virus administered is verified by titrating replicate samples on Vero cells. Clinical monitoring General health observations are performed on each animal from the day of arrival until the end of the study at least once daily (during normal servicing procedures). Each animal is weighed daily beginning one day prior to infection (day -1). Data analysis and statistical methods Survival proportions and survival times and change in bodyweight (Area Under the Curve) are compared to the corresponding control group using Fisher’s exact test, log- rank and Welch's t-test, respectively. All groups are compared to the vehicle control group. P values are adjusted according to Bonferroni (for three comparisons to vehicle) followed by a stepwise approach within antibody (starting with the highest dose and conditionally testing a lower dose if the previous step was statistically significant). Combination index Survival dose response curves are fitted for each of the treatments (First or Second antibodies or the composition comprising the combination) and the ED50is estimated. The efficacy of the combination is then compared to the First and Second antibodies by calculation of the combination index. Survival Prophylactic treatment with the First or Second antibodies or the composition comprising the combination (as indicated in Table 8) compared to the control group provides statistically significant protection against mortality and a significant improvement in survival time compared to the control group. Body weight Change in bodyweight is analyzed using an Area Under the Curve (AUC) analysis in which the last observed body weight is carried forward if a mouse died / is euthanized during the study. The weight per mouse at day 0 is used as baseline and weight change is determined relative to baseline with the net AUC defined as the summation of the area above and below the baseline using the percentage change per day. Prophylactic treatment with the composition comprising the combination (as indicated in Table 8) provides a statistically significant reduction in weight loss, compared to the control group. Conclusion In this SARS-CoV-2 Delta mouse model, the prophylactic intranasal administration of the composition comprising the combination (as indicated in Table 8) according to the invention provides significant improvement in survival and a reduction in body weight loss compared with Control Group. The outcome of the combination index is suggestive of at least a comparable, an additive or potentially synergistic effect for the combination compared to the First or Second antibodies administered alone. Example 7: ELISA binding assessment of an antibody according to the invention The objective of this study was to assess the binding of the antibody against different Corona Spike antigens, a variety of alpha and beta coronaviruses. Binding was tested in an enzyme-linked immunosorbent assay (ELISA). Briefly, a Spike antigen was used to coat the surface of a microwell of an ELISA plate. The antibody was then added in decreasing concentration to the coated and pre-blocked microwell surface in duplicates, attaching to the coated antigen. A detection antibody was added, labeled with horse radish peroxide (HRP), that then generates a colorimetric signal upon addition of the substrate. The readout was optical density and reflects binding. The antibody was assayed in duplicate against a number of alpha and beta coronavirus spike antigens, including but not limited to SARS-CoV-2 Delta, Omicron XBB.1.5 and human coronavirus NL63. The antibody was tested in comparison to other anti-S1 antibodies in the range of 10.0 - 0.000002 nM. Half maximal effective concentration (EC50) was calculated for each antibody on each antigen as an estimate of binding affinity. Table 10: ELISA EC50values (nM) for the antibody according to invention. N / D = no EC50value was determined, due to lack of binding The ELISA binding assay (Table 10) shows that the antibody according to invention was able to effectively bind all tested Spike antigens from alpha and beta coronaviruses, including SARS-CoV-2 Delta, Omicron XBB.1.5 and hCoV NL63. The anti-S1 antibodies tested only bound the SARS-CoV-2 Delta, as expected from literature and did not show breadth amongst alpha coronavirus NL63. The isotype control antibody did not show any binding to the coronavirus antigens. Example 8. Affinity binding assessment by MSD of an antibody according to the invention The objective of this study was to assess relative binding affinity against Spike antigens in a multiplexed way, with very high specificity and low sample input. Therefore, an antibody was tested in a multiplexed assay, Meso Scale Discovery (MSD), which uses electrochemiluminescent labels that were conjugated to detection antibodies. In this assay, up to ten trimeric viral antigen are separately printed onto a spot each well of the plate, allowing for a multiplexed assay readout. The antibody according to the invention bind the viral antigens through Fab-mediated recognition, then an anti-human IgG Sulfo- Tag detection antibody is added, recognizing human IgG Fab. Upon addition of read buffer containing substrate, and running a current through the plate electrodes, an electro- (current) chemi- (buffer substrate) luminescent (light) cascade is initiated which results in light emission. The intensity of emitted light is measured per spot, revealing bound levels of analyte. The antibody was assayed in duplicate against Spike antigens of SARS- CoV-2, SARS-CoV-1, MERS, hCoV NL63, hCoV HKU, hCoV OC43 and hCoV 229E (V- Plex COVID-19 Coronavirus Panel 3 (IgG) Kit cat# K15399U-2) (Table 11), as well as a set of Omicron variants (V-Plex SARS-CoV-2 Panel 34 (IgG) Kit cat# K15690U-2) in a separate assay (Table 12). The antibody was tested in a dilution range starting from 555 ng / ml for the Panel 3 and 10 ng / ml in the Omicron Panel 24 kit. Light emission from the MSD sulfo-tag antibody was quantified with MSD Discovery workbench, calibration curves were used to calculate antibody concentrations, by fitting the raw electrochemiluminescent units (eCLU) from the calibrators to a logistic regression for curve fitting (Sigmoidal, 4PL, X = conc), and the model asymptotes were constrained to the lower limit of detection (LLOQ) and the upper limit of detection (ULOQ). The concentration (ng / ml) corresponding to the midpoint of the dynamic range (that is the range between the lower and upper limit of quantification, LLOQ and ULOQ) was reported. Table 11: Antibody concentrations corresponding to the midpoint of the dynamic range (LOQ+ULOQ) / 2 (ng / ml) for the antibody according to the invention against different alpha and beta coronaviruses is shown. N / D = antibody concentration could not be determined. The MSD binding array (see Table 11) showed that the antibody was able to effectively bind Spike antigens from beta coronaviruses SARS-CoV-2, SARS-CoV-1, MERS, HKU1 and OC43. Alpha coronaviruses including 229E and NL63 were bound as well. The antibody did not bind the SARS-CoV-2 receptor binding domain (RBD) on the S1 part of the Spike used in this study. On the contrary, the anti-S1 antibody tested here bound well the RBD domain and the wildtype SARS-CoV-2, as expected from literature and did not show breadth amongst other coronaviruses. This suggests that the antibody according to invention shows breadth in binding across all tested beta and alpha coronaviruse Spikes, while the anti-RBD antibody only bound SARS-CoV-2 Spike and RBD domain. The isotype control did not show any binding to the coronavirus antigens Table 12: Antibody concentrations corresponding to the midpoint of the dynamic range (LOQ+ULOQ) / 2 (pg / ml) for the antibody according to the invention against different SARS-CoV-2 Omicron viruses is shown. N / D = antibody concentration could not be determined. The MSD binding array showed that the antibody according to invention can bind all Omicron variants tested in this assay at high concentrations up to 10 ng / ml (Table 12), therefore retaining activity among the tested Omicron mutants, as also confirmed for XBB.1.5 in the ELISA binding assay (Table 10). While the anti-S1 control antibody bound SARS-CoV-2 Spike at a lower concentration than the antibody according to invention, the earlier Omicron mutants were only bound at high extrapolated concentrations, indicating lower affinity for these mutants and the later Omicron mutants such as BQ.1 and XBB.1 were not bound. This indicates that the antibody according to invention was able to bind to the latest Omicron mutants while the anti-RBD antibody did not bind these variants. The negative isotype control antibody did not show any binding to the coronavirus antigens.. Example 9. Live virus neutralization of an antibody according to the invention The objective of this study was to assess the ability of an antibody to neutralize live corona viruses. The antibody was tested for functional activity in a live virus microneutralization assay against MERS, SARS-CoV-1 and SARS-CoV-2 Wuhan. Briefly, dilution series of an antibody were pre-incubated with the corresponding virus and then added to the respective cell line (Vero: MERS and SARS-CoV-1, SARS-CoV-2: Vero E6 cells) in quadruplicates. After incubation, cells were fixed, stained with an anti-nucleocapsid antibody, and an enzymatically tagged detection antibody was added. Colored precipitate signaling nucleocapsid presence was read out via an Immunospot analyzer and 50% inhibitory concentration (IC50), was reported via the Zielinska method (REF: https: / / doi.org / 10.1186 / 1743-422X-2-84). The antibody was tested for neutralizing activity in the range of 0.025 to 500 µg / ml. Table 13: Live virus neutralization assay. IC50 values in ug / ml are displayed for the antibody according to invention against three different beta coronaviruses. A pooled convalescent serum from SARS-CoV-2 patients was used as a comparator and SARS-CoV- 2 positive control, MN50titers are shown. N / D = IC50could not be determined Overall, the antibody according to invention was able to neutralize the tested viruses SARS-CoV-1, SARS-CoV-2 and MERS at varying concentrations (see Table 13), with the lowest IC50concentrations for SARS-CoV-1. This confirms that the antibody has neutralizing activity across these beta coronaviruses, as indicated by the binding assessment via MSD (Table 11). The positive serum control for SARS-CoV-2 requires a high MN50 titer. Example 10. Pseudovirion neutralization of an antibody according to the invention The objective of this study was to assess the ability of an antibody to neutralize different pseudotyped virus particles. The advantage over a live virus assay was that pseudotyped viruses can be used at a lower biosafety level laboratory and new variants of concern can be produced and tested more rapidly, allowing for broader testing across variants of concern or interest. Briefly, pseudovirions were produced by co-transfecting virus expression plasmids with the pHIV-1NL43 ΔEnv-NanoLuc reporter virus plasmid in HEK293T cells. Then, dilution series of the antibody were pre-incubated with the corresponding pseudovirus and then added to HEK 293T cells expressing ACE2, the entry receptor for SARS-CoV-2, SARS-CoV-1 and NL63. For hCoV 229E, the diluted antibody mixed with virus was added to Huh7 cells which express the aminopeptidase N (APN receptor which facilitates entry of hCoV 229E into host cells. After incubation, cells were washed and lysed to measure the luciferase activity in cell lysates using the Nano-Glo Luciferase Assay System and GloMax system, with a readout of relative light units (RLUs). The 50% inhibitory concentrations (IC50) were determined as the antibody concentration at which infectivity was inhibited by 50% using a four Parameter Logistic Regression (4PL) curve fit. The bispecific antibody was tested for neutralizing activity in the range of 0.0042 to 250 µg / ml against SARS-CoV-1, SARS-CoV-2 Wuhan, Delta, Omicron BA4, Omicron BQ.1.1, Omicron XBB.1, hCoV NL63 and hCoV 229E. Table 14: Pseudovirion neutralization assay. IC50 values in ug / ml were displayed for the anti-stem helix antibody against different alpha and beta coronaviruses. For multiple runs, the geometric mean with the 95% normal range is shown. Overall, the antibody according to invention was able to neutralize all tested alpha and beta viruses at varying concentrations (see Table 14), with an overall trend of higher IC50 concentrations for the Omicron variants. This indicates that the antibody according to invention shows neutralization breath across alpha and beta coronaviruses, as expected based on the binding data. Example 11. Epitope mapping of an antibody according to the invention The goal of this study was to precisely determine the amino acid sequence that the antibody according to the invention binds to in the Spike protein across different alpha and beta coronaviruses. The method includes mapping of linear epitopes using libraries of overlapping synthetic peptides from the spike protein. Briefly, linear epitopes of the sequence of interest were synthesized directly on a solid chip, generating a library of linear mimics, aiding identification of the correct amino acid sequence of the target antibody. The library of peptides consists of overlapping 15-amino acid fragments, with an overlap of 14 amino acids. Binding of the antibody to each of the synthesized peptide chips was tested in an enzyme-linked immunosorbent assay (ELISA) assay via incubation of the peptide arrays with antibody solutions. After washing, peptide arrays were incubated with an antibody peroxidase conjugate and substrate was added, and the reaction was then stopped using hydrogen peroxide. Colour development was measured and intensity was reported. The antibody according to invention bound the peptide array of alpha and beta coronaviruses in a specific epitope of a 10- 20 amino acids (see Figure 6). The method allowed for a high confidence in the epitope definition, with certain variance in the outer areas of the epitope, indicated by asterisk for the respective strain. Example 13. Affinity binding assessment by MSD of a bispecific antibody The objective of this study was to assess relative binding affinity against Spike antigens in a multiplexed way, with very high specificity and low sample input. Therefore, an antibody was tested in a multiplexed assay, Meso Scale Discovery (MSD), which uses electrochemiluminescent labels that were conjugated to detection antibodies. The first parental antibody (“Parental mAb 1”) has the following CDRs as described in SEQ ID Numbers:013, 170, 266, 386, 439, and 584. The second parental antibody (“Parental mAb 2”) has the following CDRs as described in SEQ ID Numbers: 650, 651, 652, 653, 654, and 655. The bi-specific antibody according to the invention has a first Fab that comprises a sequence comprising any one or more of SEQ ID Numbers: 013, 170, 266, 386, 439, and 584; the second Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 650, 651, 652, 653, 654, and 655. Three versions of bispecific antibodies have been produced and tested, all with the combination of the Parental mAb 1 and Parental mAb 2. In this assay, up to ten trimeric viral antigens are separately printed onto a spot each well of the plate, allowing for a multiplexed assay readout. The antibody according to the invention bind the viral antigens through Fab-mediated recognition, then an anti-human IgG Sulfo-Tag detection antibody is added, recognizing human IgG Fab. Upon addition of read buffer containing substrate, and running a current through the plate electrodes, an electro- (current) chemi- (buffer substrate) luminescent (light) cascade is initiated which results in light emission. The intensity of emitted light is measured per spot, revealing bound levels of analyte. The antibody was assayed in duplicate against Spike antigens of SARS-CoV-2, SARS-CoV-1, MERS, hCoV NL63, hCoV HKU, hCoV OC43 and hCoV 229E (V-Plex COVID-19 Coronavirus Panel 3 (IgG) Kit cat# K15399U-2) (Table 20), as well as a set of Omicron variants (V-Plex SARS-CoV-2 Panel 34 (IgG) Kit cat# K15690U-2) in a separate assay (Table 21). The antibody was tested in a dilution range starting from 555 ng / ml for the Panel 3 and 10 ng / ml in the Omicron Panel 24 kit. Light emission from the MSD sulfo-tag antibody was quantified with MSD Discovery workbench, calibration curves were used to calculate antibody concentrations, by fitting the raw electrochemiluminescent units (eCLU) from the calibrators to a logistic regression for curve fitting (Sigmoidal, 4PL, X = conc), and the model asymptotes were constrained to the lower limit of detection (LLOQ) and the upper limit of detection (ULOQ). The concentration (ng / ml) corresponding to the midpoint of the dynamic range (that is, the range between the lower and upper limit of quantification, LLOQ and ULOQ) was reported. Table 20: Antibody concentrations corresponding to the midpoint of the dynamic range (LOQ+ULOQ) / 2 ng / ml ) for the bispecific antibodies compared to the parental antibodies against different SARS-CoV-2 Omicron variants. N / D = antibody concentration could not be determined. The MSD binding array (see Table 20) showed that the bispecific antibodies were able to effectively bind all Spike antigens from alpha and beta coronaviruses. Alpha coronavirus NL63 was not bound by the Parental mAb 2 anti-stem helix antibody, but only by the anti-fusion peptide Parental mAb 1 and the bispecific antibodies, albeit at slightly higher concentrations than the Parental antibody 1. Alpha coronavirus 229E was bound by all tested antibodies, with lower concentrations for Parental mAb 1. The SARS-CoV-2 Spike RBD antigen was only bound at high concentrations by the Parental mAb 2 (stem-helix mAb) and the bispecific antibodies. The control anti-S1 mAb only bound SARS-CoV-2 Spike and RBD, at low concentrations. The data suggests that the bispecific antibodies retain the binding capacity from each parental antibody, here demonstrated by the ability to utilize the Fab arm of the Parental mAb 1 and retaining alpha coronavirus binding activity. Table 21: Antibody concentrations corresponding to the midpoint of the dynamic range (LOQ+ULOQ) / 2 (pg / ml) for the bispecific antibodies compared to the Parental antibodies against different SARS-CoV-2 Omicron variants. N / D = antibody concentration could not be determined. The MSD binding array (see Table 21) showed that the three bispecific antibodies were able to effectively bind all Spike antigens from SARS-CoV-2 Omicron variants at varying concentrations. While only the Parental mAb 2 retains efficient binding against later Omicron variants (< 1000 pg / ml) and the Parental mAb 1 requires high antibody concentrations, the bispecific antibodies retain binding at low concentrations, suggesting that the bispecific antibodies can leverage the Fab arm of Parental mAb 2. Example 14: Live virus neutralization of a bispecific antibody The objective of this study was to assess the ability of the bispecific antibody to neutralize live corona viruses and pseudovirions. The bispecific antibody was tested for functional activity in a live virus microneutralization assay against MERS, SARS-CoV-1, SARS- CoV-2 Wuhan, Delta and Omicron BA.4 / 5. The first parental antibody (“Parental mAb 1”) has the following CDRs as described in SEQ ID Numbers:013, 170, 266, 386, 439, and 584. The second parental antibody (“Parental mAb 2”) has the following CDRs as described in SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. The bispecific antibody according to the invention has a first Fab that comprises a sequence comprising any one or more of SEQ ID Numbers: 013, 170, 266, 386, 439, and 584; the second Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. The bispecific antibody BISPECIFIC 1 comprises the first Fab and the second Fab as described above. Briefly, dilution series of antibodies were pre-incubated with the corresponding virus and then added to the respective cell line (Vero: MERS and SARS-CoV-1, all other Vero E6 cells). After incubation, cells were fixed, stained with an anti-nucleocapsid antibody, and an enzymatically tagged and a detection antibody was added. Colored precipitate signaling nucleocapsid presence was read out via an Immunospot analyzer and 50% inhibitory concentration (IC50), was reported. The bispecific antibody was tested for neutralizing activity in the range of 0.02 to 500 µg / ml compared to the individual control antibodies. Table 22: Live virus neutralization assay. IC50 values in ug / ml are displayed for against three different beta coronaviruses. Parental antibodies are assayed alongside the bispecific antibody as comparator. Overall, the bispecific antibody was able to neutralize the tested viruses SARS-CoV-1, SARS-CoV-2 Wuhan, Delta and Omicron BA.4 / 5 and MERS at varying concentrations (see Table 22). The anti-stem helix Parental antibody 2 was able to neutralize SARS-CoV-2 Wuhan and MERS at lower IC50concentrations compared to the anti-fusion peptide antibody Parental mAb 1, this trend was also observed for the bispecific antibody, indicating that the antibody can leverage the anti-stem helix Fab arm. For SARS-CoV-2 Delta, Omicron BA4.5 and SARS-CoV-1, the parental and the bispecific antibodies neutralize at similar IC50concentrations. Overall, this indicates that the bispecific antibody retains affinity from both parental Fab arms and retain neutralizing activity across tested beta coronaviruses. Example 15: Pseudovirion neutralization of a bispecific antibody The pseudovirion neutralization assay was performed against pseudotyped virus particles. The first parental antibody (“Parental mAb 1”) has the following CDRs as described in SEQ ID Numbers: 013, 170, 266, 386, 439, and 584. The second parental antibody (“Parental mAb 2”) has the following CDRs as described in SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. The bi-specific antibody according to the invention has a first Fab that comprises a sequence comprising any one or more of SEQ ID Numbers: 013, 170, 266, 386, 439, and 584; the second Fab comprises a sequence comprising any one or more of SEQ ID Numbers: 650, 651, 652, 653, 654 and 655. The bispecific antibody BISPECIFIC 1 comprises the first Fab and the second Fab as described above. The advantage over a live virus assay was that pseudotyped viruses can be used at a lower biosafety level laboratory and new variants of concern can be produced and tested more rapidly. Briefly, pseudovirions were produced by co-transfecting virus expression plasmids with the pHIV-1NL43 ΔEnv-NanoLuc reporter virus plasmid in HEK293T cells. Then, dilution series of antibodies were pre-incubated with the corresponding pseudovirus and then added to HEK 293T cells expressing ACE2, the entry receptor for SARS-CoV-2, SARS-CoV-1 and NL63. After incubation, cells were washed and lysed to measure the luciferase activity in cell lysates using the Nano-Glo Luciferase Assay System and GloMax system. The 50% inhibitory concentrations (IC50) were determined as the antibody concentration at which infectivity was inhibited by 50% using a four Parameter Logistic Regression (4PL) curve fit. The bispecific antibody was tested for neutralizing activity in the range of 0.01 to 250 µg / ml compared to the individual control antibodies against SARS-CoV-2 Wuhan, Delta, Omicron BA4 / 5, BQ.1 and XBB.1, hCoV NL63 and hCoV 229E. Table 23: Pseudovirion neutralization assay. IC50values in ug / ml were displayed for the anti-stem helix and anti- fusion peptide antibodies against different beta coronaviruses. For multiple runs, the geometric mean with 95% normal range is shown. The Pseudovirion neutralization assay (see Table 23) shows that for the Omicron variants, especially the ones arising later such as XBB.1.1, the Parental antibody 2 according to invention was able to neutralize at lower concentrations than the anti-fusion peptide Parental mAb 1, with the bispecific antibody retaining the neutralizing activity with IC50 concentrations in the middle of each Parental mAb, except for SARS-CoV-2 Wuhan, which was neutralized by the bispecific antibody at the lowest concentration compared to the Parental antibodies. The overall trends of the bispecific antibody retaining neutralizing activity of its parental antibodies was confirmed from the live virus assay (Table 22). This indicates that the bispecific antibody retains neutralizing affinity from each Fab arm of the parental antibodies.

Claims

CLAIMS 1. An anti-coronavirus, preferably anti-SARS-CoV-2 bispecific antibody or an antigen binding fragment thereof, having a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 and a second Fab capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: SEQ ID Numbers: 662, 663, 664, 665, 666 to 667.

2. A bispecific antibody or an antigen binding fragment thereof according to Claim 1, comprising a first Fab capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein the first Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: 013, 170, 266, 368, 439 and / or 584 and wherein the second Fab comprises a sequence comprising any one or more of preferred SEQ ID Numbers: SEQ ID Numbers: 662, 663, 664, 665, 666 and / or 667.

3. A bispecific antibody or an antigen binding fragment thereof according to Claims 1 or 2, comprising a first Fab specifically binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and a second Fab specifically binding to the stem helix of a coronavirus, preferably SARS-CoV-2, characterized in that: a.) the first Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and b.) the second Fab comprises a heavy chain variable region comprising as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and a light chain variable region comprising as CDRs a Light Chain CDR1 region of SEQ IDNO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO:

667.

4. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 3, comprising: a) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, and b) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody or an antigen binding fragment thereof, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein constant domains CL and CH1 from the antibody or an antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, are replaced by each other.

5. A bispecific antibody or an antigen binding fragment thereof according to Claim 4, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and the VL domain of the antibody or the antigen binding fragment thereof that is capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO: 667.

6. A bispecific antibody, or an antigen binding fragment thereof according to any of Claims 1 to 3, comprising: a) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein constant domains CL and CH1 from the antibody that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2 are replaced by each other.

7. A bispecific antibody or an antigen binding fragment thereof according to Claim 6, wherein the VH domain of the antibody or the antigen binding fragment thereof that is capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 013, a Heavy Chain CDR2 region of SEQ ID NO: 170 and a Heavy Chain CDR3 region of SEQ ID NO: 266 and the VL domain of the antibody capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 368, a Light Chain CDR2 region of SEQ ID NO: 439 and a Light Chain CDR3 region of SEQ ID NO: 584, and wherein the VH domain of the antibody capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs, a Heavy Chain CDR1 region of SEQ ID NO: 662, a Heavy Chain CDR2 region of SEQ ID NO: 663 and a Heavy Chain CDR3 region of SEQ ID NO: 664 and the VL domain of the antibody capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, comprises as CDRs a Light Chain CDR1 region of SEQ ID NO: 665, a Light Chain CDR2 region of SEQ ID NO: 666 and a Light Chain CDR3 region of SEQ ID NO:

667.

8. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 3, comprising:a) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody, capable of binding to the fusion peptide of a coronavirus, preferably SARS-CoV-2; and b) A light chain comprising VL-CL domains and a heavy chain comprising VH-CH1- CH2-CH3 domains of an antibody, capable of binding to the stem helix of a coronavirus, preferably SARS-CoV-2, wherein domains VL-CL and VH-CH1 from the antibody that specifically binds to the fusion peptide of a coronavirus, preferably SARS-CoV-2, are replaced by each other.

9. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 8, wherein the first Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO:

640.

10. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 8, wherein the second Fab comprises a heavy chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO:

688.

11. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 8, wherein the first Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO:

641.

12. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 8, wherein the second Fab comprises a light chain variable region having an amino acid sequence that is at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical,at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to the amino acid sequences set forth in SEQ ID NO:

689.

13. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 8, wherein the bispecific antibody or antigen binding fragment thereof is selected from anyone of the group comprising a full-length antibody, a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibodies, scFv, scFv- Fc, bi, tri or tetra-valent antibodies, Bis-scFv, diabodies, triabodies, tetrabodies and epitope binding fragments thereof.

14. A method for the production of a bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 13, comprising a) culturing a host cell, comprising an expression vector, comprising a polynucleotide encoding a bispecific antibody or an antibody fragment according to any one of the preceding Claims under conditions which permit the production of said bispecific antibody or an antigen binding fragment thereof, and b) isolating said bispecific antibody or an antigen binding fragment thereof.

15. A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or a light chain variable region of the bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 13, preferably wherein the nucleic acid molecule is an isolated nucleic acid molecule.

16. A nucleic acid molecule comprising a nucleic acid sequence, wherein the nucleic acid sequence encodes the bispecific antibody or antigen binding fragment thereof, a heavy chain variable region and / or light chain variable region of the bispecific antibody or the antigen binding fragment thereof according to any of Claims 1 to 65 and Claim 15, wherein the nucleic acid sequence comprises at least anyone of: (i) a first nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.013, or a first nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 013,(ii) a second nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 170, or a second nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO.170, (iii) a third nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.266, or a third nucleic acid sequence encoding the amino acid sequence having at most 1, 2 or 3 amino acids different from SEQ ID NO. 266, (iv) a fourth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.368, or a fourth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3 or 4 amino acids different from SEQ ID NO.368, (v) a fifth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 439, or a fifth nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 439, (vi) a sixth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.584, or a sixth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, or 4 amino acids different from SEQ ID NO. 584, (vii) a seventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 662, or a seventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 662, (viii) an eighth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 663, or an eighth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO.663, (ix) a nineth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.664, or a nineth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, 3, 4, or 5 amino acids different from SEQ ID NO. 664, (x) a tenth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO.665, or a tenth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, or 3 amino acids different from SEQ ID NO. 665, (xi) an eleventh nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 666, or an eleventh nucleic acid sequence encoding the amino acid sequence having at most 1 or 2 amino acids different from SEQ ID NO. 666, and (xii) a twelfth nucleic acid sequence encoding the amino acid sequence as set forth in SEQ ID NO. 667, or a twelfth nucleic acid sequence encoding the amino acid sequence having at most 1, 2, or 3 amino acids different from SEQ ID NO. 667.

17. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 13 for use in a method of treating a coronavirus infection in a subject.

18. A composition comprising the bispecific antibody and / or an antigen binding fragment thereof according to any of Claims 1 to 13.

19. A composition according to Claim 18 further comprising a second medicament, for simultaneous, separate, or sequential administration.

20. A composition according to Claim 19, wherein the second medicament comprises a second antibody or antigen binding fragment thereof.

21. A composition according to Claim 19, wherein the second medicament comprises a bispecific antibody or bispecific antigen binding fragment thereof.

22. A composition according to Claim 19, wherein the composition further comprises a pharmaceutically acceptable excipient or carrier.

23. A composition according to Claim 18, for use in inhibiting and / or treating a coronavirus infection in a subject, preferably, a SARS-CoV-1 or SARS-CoV-2 infection in a subject, comprising an effective amount of the bispecific antibody or an antigen binding fragment thereof, nucleic acid molecule, or vector, and optionally a pharmaceutically acceptable excipient or carrier.

24. The composition of Claim 18, for use as a medicament.

25. An inhaler device comprising the composition of Claim 18.

26. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 13, wherein the bispecific antibody or an antigen binding fragment thereof is bivalent.

27. A bispecific antibody or an antigen binding fragment thereof according to any of Claims 1 to 13, wherein the bispecific antibody or antigen binding fragment thereof is capable of binding to the stem helix and / or the fusion peptide of at least one of an α-coronavirus, β-coronavirus, γ-coronavirus, and δ-coronavirus, preferably at least an α-coronavirus and / or a β-coronavirus.

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