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Structure of Parvovirus B19 Decorated by Fabs from a Human Antibody.

Author: KloseThomas, LiuYue, ModrowSusanne, RossmannMichael G, SunYingyuan

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.
Research Support, U.S. Gov't, Non-P.H.S.Research funding provided by US government agencies other than the Public Health Service.

Overview

This study presents the first cryo-EM structure of a B19 virus-like particle complexed with a neutralizing antibody Fab. This structure identifies the antigenic residues on the B19 capsid and provides insights into host recognition of the virus, contributing to the development of vaccines and therapeutic antibodies for B19 infections.
Paper Details　
Original Abstract of the Article :
Parvovirus B19, one of the most common human pathogens, is a small DNA virus that belongs to the <i>Parvoviridae</i> As a result of previous infections, antibodies to B19 are present in most adults. B19 has a strong tropism to erythroid progenitor cells and is able to cause a series of medical condi...See full text at original site
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引用元：
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6475792/

データ提供：米国国立医学図書館（NLM）

Structure of Parvovirus B19 Decorated by Fabs from a Human Antibody

Parvovirus B19 is a common human pathogen that can cause a range of medical conditions. This study presents the first cryo-electron microscopy (cryo-EM) structure of a B19 virus-like particle (VLP) complexed with the antigen-binding fragment (Fab) of a human neutralizing antibody, 860-55D. The authors provide a high-resolution structural characterization of the B19-antibody complex, identifying the antigenic residues on the surface of the B19 capsid.

Structural Insights into B19-Antibody Interactions

The study found that antibody 860-55D bridges the capsid of B19 by binding to a quaternary structure epitope formed by residues from three neighboring VP2 capsid proteins. This structural information provides a detailed understanding of the molecular interactions between B19 and a human neutralizing antibody, paving the way for the development of new antiviral therapies and vaccines.

Understanding the Mechanisms of B19 Infection

Understanding the structural basis of B19-antibody interactions is crucial for developing effective therapies and vaccines for this common pathogen. The study's findings contribute significantly to our knowledge of B19 infection and its potential for treatment.

Dr. Camel's Conclusion

This research, like a skilled archaeologist uncovering ancient secrets in the desert sands, reveals the intricate structure of B19-antibody interactions. The study's findings provide a foundation for developing new strategies to combat B19 infection and its associated diseases.

Date :
  1. Date Completed 2020-01-28
  2. Date Revised 2020-03-09
Further Info :

Pubmed ID

30787153

DOI: Digital Object Identifier

PMC6475792

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Languages

English

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