Request ID: cfg_rRequest_1182
Status
:
Approved
Project Description
:
Characterization of the glycan binding properties of the H1N1 mutant viruses
CFG Member
:
Not Consortium Member
Requester First Name
:
Scott
Requester Last Name
:
Hensley
Head of Lab First Name
:
Jonathan
Head of Lab Last Name
:
Yewdell
Assigned First Name
:
Jonathan
Assigned Last Name
:
Yewdell
Requester Email
:
hensleys@niaid.nih.gov
Requester Interest
:
Information not entered/not applicable.
Request Date [yyyy-mm-dd]
:
2007-10-16
Institution
:
National Institute of Allergy and Infectious Diseases, National Institutes of Health
Shipping Address
:
Bldg 33, Room 2E13
33 North Drive
Bethesda, MD 20892-3209
(301) 496-2216
Comments
:
Information not entered/not applicable.
CFG Core
:
H
Resource Type
:
Glycoarray
Amount Requested
:
Information not entered/not applicable.
Date that your RNA/GBP samples will be sent to the core [yyyy-mm-dd]
:
2007-12-17
Experiment to be conducted
:
In order to escape neutralizing antibodies, influenza viruses accumulate mutations in the hemagglutinin and neuraminidase proteins. We have generated escape mutants by culturing H1N1 (PR8) in ovo in the presence of H1-specific monoclonal antibodies or in vivo by passaging H1N1 in vaccinated mice. Based on crude receptor binding studies, a number of the mutants appear to bind to sialic acid receptors with higher avidity. The goal of the present study is to characterize the glycan binding properties of these H1N1 mutant viruses. Specifically, we will address the extent to which the mutants demonstrate altered carbohydrate specificity. These studies have broad implications for antigenic variation in the hemagglutinin protein, vaccine development, and cross-species adaptation of influenza viruses.
Within Scope of Consortium
:
Y
If yes, indicate the person responsible for inputing data into core B
:
Information not entered/not applicable.
GBP being Addressed
:
Information not entered/not applicable.
Specifc aims being addressed
:
Define the specificity and affinity for carbohydrate ligands. Identify the ligand(s) that mediate GBP binding.