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The mechanism of henipavirus fusion: Examining the relationships between the attachment and fusion glycoproteins

Content Provider	Springer Nature Link
Author	Hickey, Andrew C. Broder, Christopher C.
Copyright Year	2009
Abstract	The henipaviruses, represented by Nipah virus and Hendra virus, are emerging zoonotic viral pathogens responsible for repeated outbreaks associated with high morbidity and mortality in Australia, Southeast Asia, India and Bangladesh. These viruses enter host cells via a class I viral fusion mechanism mediated by their attachment and fusion envelope glycoproteins; efficient membrane fusion requires both these glycoproteins in conjunction with specific virus receptors present on susceptible host cells. The henipavirus attachment glycoprotein interacts with a cellular B class ephrin protein receptor triggering conformational alterations leading to the activation of the viral fusion (F) glycoprotein. The analysis of monoclonal antibody (mAb) reactivity with G has revealed measurable alterations in the antigenic structure of the glycoprotein following its binding interaction with receptor. These observations only appear to occur with full-length native G glycoprotein, which is a tetrameric oligomer, and not with soluble forms of G (sG), which are disulfide-linked dimers. Single amino acid mutations in a heptad repeat-like structure within the stalk domain of G can disrupt its association with F and subsequent membrane fusion promotion activity. Notably, these mutants of G also appear to confer a post-receptor bound conformation implicating the stalk domain as an important element in the G glycoprotein’s structure and functional relationship with F. Together, these observations suggest fusion is dependent on a specific interaction between the F and G glycoproteins of the henipaviruses. Further, receptor binding induces measurable changes in the G glycoprotein that appear to be greatest in respect to the interactions between the pairs of dimers comprising its native tetrameric structure. These receptor-induced conformational changes may be associated with the G glycoprotein’s promotion of the fusion activity of F.
Starting Page	110
Ending Page	120
Page Count	11
File Format	PDF
ISSN	16740769
Journal	Virologica Sinica
Volume Number	24
Issue Number	2
e-ISSN	1995820X
Language	English
Publisher	SP Wuhan Institute of Virology, CAS
Publisher Date	2009-04-14
Publisher Place	Heidelberg
Access Restriction	Subscribed
Subject Keyword	Hendra virus Nipah virus Henipavirus Paramyxovirus Viral entry Microbial Genetics and Genomics Microbiology Biochemistry Oncology Medical Microbiology Virology
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Virology Immunology Molecular Medicine

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