6WRP
Crystal Structure of PI3-E12 Fab, An Antibody Against Human Parainfluenza Virus Type III
Summary for 6WRP
Entry DOI | 10.2210/pdb6wrp/pdb |
Descriptor | PI3-E12 Fab Heavy Chain, PI3-E12 Fab Light Chain, DI(HYDROXYETHYL)ETHER, ... (7 entities in total) |
Functional Keywords | antibody, fab, immune system |
Biological source | Homo sapiens More |
Total number of polymer chains | 2 |
Total formula weight | 49505.34 |
Authors | Weidle, C.,Pancera, M. (deposition date: 2020-04-29, release date: 2021-05-05, Last modification date: 2023-10-18) |
Primary citation | Boonyaratanakornkit, J.,Singh, S.,Weidle, C.,Rodarte, J.,Bakthavatsalam, R.,Perkins, J.,Stewart-Jones, G.B.E.,Kwong, P.D.,McGuire, A.T.,Pancera, M.,Taylor, J.J. Protective antibodies against human parainfluenza virus type 3 infection. Mabs, 13:1912884-1912884, 2021 Cited by PubMed Abstract: Human parainfluenza virus type III (HPIV3) is a common respiratory pathogen that afflicts children and can be fatal in vulnerable populations, including the immunocompromised. There are currently no effective vaccines or therapeutics available, resulting in tens of thousands of hospitalizations per year. In an effort to discover a protective antibody against HPIV3, we screened the B cell repertoires from peripheral blood, tonsils, and spleen from healthy children and adults. These analyses yielded five monoclonal antibodies that potently neutralized HPIV3 . These HPIV3-neutralizing antibodies targeted two non-overlapping epitopes of the HPIV3 F protein, with most targeting the apex. Prophylactic administration of one of these antibodies, PI3-E12, resulted in potent protection against HPIV3 infection in cotton rats. Additionally, PI3-E12 could also be used therapeutically to suppress HPIV3 in immunocompromised animals. These results demonstrate the potential clinical utility of PI3-E12 for the prevention or treatment of HPIV3 in both immunocompetent and immunocompromised individuals. PubMed: 33876699DOI: 10.1080/19420862.2021.1912884 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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