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Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies.
- Source :
-
Nature microbiology [Nat Microbiol] 2024 Aug; Vol. 9 (8), pp. 2128-2143. Date of Electronic Publication: 2024 Jun 10. - Publication Year :
- 2024
-
Abstract
- Human parainfluenza virus type 3 (hPIV3) is a respiratory pathogen that can cause severe disease in older people and infants. Currently, vaccines against hPIV3 are in clinical trials but none have been approved yet. The haemagglutinin-neuraminidase (HN) and fusion (F) surface glycoproteins of hPIV3 are major antigenic determinants. Here we describe naturally occurring potently neutralizing human antibodies directed against both surface glycoproteins of hPIV3. We isolated seven neutralizing HN-reactive antibodies and a pre-fusion conformation F-reactive antibody from human memory B cells. One HN-binding monoclonal antibody (mAb), designated PIV3-23, exhibited functional attributes including haemagglutination and neuraminidase inhibition. We also delineated the structural basis of neutralization for two HN and one F mAbs. MAbs that neutralized hPIV3 in vitro protected against infection and disease in vivo in a cotton rat model of hPIV3 infection, suggesting correlates of protection for hPIV3 and the potential clinical utility of these mAbs.<br /> (© 2024. The Author(s), under exclusive licence to Springer Nature Limited.)
- Subjects :
- Animals
Humans
Disease Models, Animal
Neutralization Tests
B-Lymphocytes immunology
Models, Molecular
Parainfluenza Virus 3, Human immunology
Parainfluenza Virus 3, Human genetics
Antibodies, Monoclonal immunology
Antibodies, Monoclonal chemistry
Antibodies, Neutralizing immunology
Antibodies, Neutralizing chemistry
Antibodies, Viral immunology
Antibodies, Viral chemistry
Sigmodontinae
Viral Fusion Proteins immunology
Viral Fusion Proteins chemistry
HN Protein immunology
HN Protein chemistry
HN Protein genetics
Respirovirus Infections immunology
Respirovirus Infections virology
Subjects
Details
- Language :
- English
- ISSN :
- 2058-5276
- Volume :
- 9
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Nature microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 38858594
- Full Text :
- https://doi.org/10.1038/s41564-024-01722-w