TY - JOUR
T1 - PIV5 M protein interaction with host protein angiomotin-like 1
AU - Pei, Zifei
AU - Bai, Yuting
AU - Schmitt, Anthony P.
N1 - Funding Information:
We thank Bob Lamb for PIV5 cDNAs, and polyclonal antibodies to PIV5 F and M proteins. We thank Steve Rubin and Biao He for mumps virus cDNAs. We are grateful to Phuong Schmitt for assistance with co-immunoprecipitation experiments, and to Megan Harrison for critical reading of the manuscript. This work was supported in part by the Middle Atlantic Regional Center of Excellence (MARCE) for Biodefense and Emerging Infectious Disease Research NIH grant AI057168 , and research grant AI070925 from the National Institute of Allergy and Infectious Diseases to A.P.S. This project is funded, in part, under a grant with the Pennsylvania Department of Health using Tobacco Settlement funds to A.P.S. The Department specifically disclaims responsibility for any analyses, interpretations or conclusions.
PY - 2010/2/5
Y1 - 2010/2/5
N2 - Paramyxovirus matrix (M) proteins organize virus assembly, functioning as adapters that link together viral ribonucleoprotein complexes and viral glycoproteins at infected cell plasma membranes. M proteins may also function to recruit and manipulate host factors to assist virus budding, similar to retroviral Gag proteins. By yeast two-hybrid screening, angiomotin-like 1 (AmotL1) was identified as a host factor that interacts with the M protein of parainfluenza virus 5 (PIV5). AmotL1-M protein interaction was observed in yeast, in transfected mammalian cells, and in virus-infected cells. Binding was mapped to a 83-amino acid region derived from the C-terminal portion of AmotL1. Overexpression of M-binding AmotL1-derived polypeptides potently inhibited production of PIV5 VLPs and impaired virus budding. Expression of these polypeptides moderately inhibited production of mumps VLPs, but had no effect on production of Nipah VLPs. siRNA-mediated depletion of AmotL1 protein reduced PIV5 budding, suggesting that this interaction is beneficial to paramyxovirus infection.
AB - Paramyxovirus matrix (M) proteins organize virus assembly, functioning as adapters that link together viral ribonucleoprotein complexes and viral glycoproteins at infected cell plasma membranes. M proteins may also function to recruit and manipulate host factors to assist virus budding, similar to retroviral Gag proteins. By yeast two-hybrid screening, angiomotin-like 1 (AmotL1) was identified as a host factor that interacts with the M protein of parainfluenza virus 5 (PIV5). AmotL1-M protein interaction was observed in yeast, in transfected mammalian cells, and in virus-infected cells. Binding was mapped to a 83-amino acid region derived from the C-terminal portion of AmotL1. Overexpression of M-binding AmotL1-derived polypeptides potently inhibited production of PIV5 VLPs and impaired virus budding. Expression of these polypeptides moderately inhibited production of mumps VLPs, but had no effect on production of Nipah VLPs. siRNA-mediated depletion of AmotL1 protein reduced PIV5 budding, suggesting that this interaction is beneficial to paramyxovirus infection.
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U2 - 10.1016/j.virol.2009.11.002
DO - 10.1016/j.virol.2009.11.002
M3 - Article
C2 - 19932912
AN - SCOPUS:73949100601
SN - 0042-6822
VL - 397
SP - 155
EP - 166
JO - Virology
JF - Virology
IS - 1
ER -