Medical Journals

The Neutralizing Antibody Response Against West Nile Virus in Naturally Infected Horses.

Authors:
  • Sánchez Melissa D
  • Pierson Theodore C
  • Degrace Marciela M
  • Mattei Lisa M
  • Hanna Sheri L
  • Del Piero Fabio
  • Doms Robert W

From: Department of Microbiology, University of Pennsylvania, 225 Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104, USA.

Virology

  • Publish Date: Mar 2007
  • ISSN: 0042-6822
  • Volume: 359
  • Issue: 2
  • Pages: 336-48
  • Medium: Print
  • Language: English
  • Citation (JAMA): Sánchez Melissa D, Pierson Theodore C, Degrace Marciela M, et al. The Neutralizing Antibody Response Against West Nile Virus in Naturally Infected Horses.. Virology Mar 2007;359:336-48

Abstract

A major neutralizing epitope (here referred to as the T332 epitope) located on the lateral surface of domain III (DIII) of the West Nile virus (WNV) envelope protein has been identified based on the analysis of murine monoclonal antibodies. However, little is known about the humoral immune response against WNV in a natural host or whether DIII in general or the T332 epitope in particular are important targets of neutralizing antibodies in vivo. To characterize the types of antibodies produced during infection with WNV, we studied a group of naturally infected horses. Using immune adsorption assays coupled with the use of virus particles bearing mutations in the T332 epitope, we found that in some animals neutralizing activity against DIII and the T332 epitope was below the limit of detection. In contrast, some animals generated a significant fraction of neutralizing activity to DIII and the T332 epitope. Thus, while antibodies to the T332 epitope did not represent a significant fraction of the total antibody response in the infected animals studied, in some horses, they comprised a significant fraction of neutralizing activity, making this an important but far from dominant neutralizing epitope. Rather, the neutralizing response to WNV generated in infected horses is both variable and polyclonal in nature, with epitopes within and outside of DIII playing important roles.

Mesh Headings (Keywords): Animals, Antibodies, Viral, Antibody Affinity, Cell Line, Epitopes, Horse Diseases, Horses, Humans, Neutralization Tests, Protein Conformation, Viral Envelope Proteins, West Nile Fever


Check for Full Text / PubMed Unique Identifier (PMID): 17055550


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


Advertisements

About | Privacy Policy | Business Solutions | Advertise | Contact | Add Healia to your site

©2012. Healia / Meredith Corporation  

Use of this site constitutes acceptance of our Terms of Service and Privacy Policy. All content on this Web site, including medical opinion and any other health-related information, is for informational purposes only and should not be used for a specific diagnosis or individual treatment plan for any situation. Use of this site and the information contained herein does not create a doctor-patient relationship. Always seek the direct advice of your doctor in connection with any questions or issues you may have regarding your own health or the health of others.