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Molecular Architecture of Viral Assembly and Bud Site Formation
Author(s) -
Stahelin Robert V,
AduGyamfi Emmanuel,
Cossell Christina M,
Soni Smita
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.939.8
Subject(s) - budding , microbiology and biotechnology , biology , capsid , cell , viral envelope , virology , viral replication , viral entry , virus , genetics
Viruses cause an array of diseases, some fatal and others a minor nuisance, some transmitted through the air and others through bodily fluids. Strides have been made in eradicating some viruses from the planet through vaccination but others such as HIV, Ebola or the Human T‐cell Leukemia virus (HTLV) lack significant treatment options or preventive vaccination. The pathogenesis of these viruses depends on infection, replication and generation of new virions. This process requires concerted action of newly synthesized viral proteins and hijacking of mammalian machinery. The generation of new virions requires budding from the host cell membrane into a new particle with the ability to infect more cells. Over the last several years the matrix proteins (MA) and capsid proteins (CA) have been implicated in association with lipid membranes and budding from the host cell to create new virions but mechanistic insight is lacking. To address basic questions underlying virion formation, we have used biochemical, biophysical, structural, cellular, and single molecule analysis to investigate how MAs bind lipid membranes and change their shape. We then map these interactions in human cells and in the formation of new virions.