Journal
JOURNAL OF VIROLOGY
Volume 78, Issue 3, Pages 1403-1410Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.78.3.1403-1410.2004
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Funding
- NHLBI NIH HHS [T32 HL007623, T32-HL07623] Funding Source: Medline
- NIAID NIH HHS [T32-AI07498, T32 AI007498] Funding Source: Medline
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The spring-loaded model stipulates that influenza virus infection is coupled to the transition of the virus hemagglutinin (HA) from a metastable conformation to a highly stable conformation at low pH. The properties of retrovirus envelope glycoproteins indicate that infection is coupled to an analogous conformational change. As a test of this hypothesis, the requirements for avian leukosis virus A (ALV-A) infection were examined. These studies indicate that, like HA, the conformation of the mature ALV-A envelope glycoprotein is metastable and that infection is linked to refolding at low pH. However, unlike HA, low-pH activation is only observed after priming by receptor. Therefore, ALV-A infection is dependent on the synergistic effects of receptor binding and low pH, suggesting that receptor binding superimposes an additional constraint on activation of ALV-A fusion that proceeds by a mechanism comparable to that of influenza virus.
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