tetano
Editor, Senior Moderator
J Virol. 2012 Oct 10. [Epub ahead of print]
The N-terminal region of IFITM3 modulates its antiviral activity through regulating IFITM3 cellular localization.
Jia R, Pan Q, Ding S, Rong L, Liu SL, Geng Y, Qiao W, Liang C.
Source
Key Laboratory of Molecular Microbiology and Biotechnology (Ministry of Education) and Key Laboratory of Microbial Functional Genomics (Tianjin), College of Life Sciences, Nankai University, Tianjin 300071, China.
Abstract
Interferon inducible transmembrane (IFITM) protein family members IFITM1, 2 and 3 restrict the infection of multiple enveloped viruses. Significant enrichment of a minor IFITM3 allele was recently reported in patients who were hospitalized for seasonal and 2009 H1N1 pandemic flu. This IFITM3 allele lacks the first amino-terminal 21 amino acids and is unable to inhibit influenza A virus. In this study, we find that deleting this 21-amino acid region relocates IFITM3 from the endosomal compartments to cell periphery. This finding likely underlies the lost inhibition of influenza A virus that completes its entry exclusively within endosomes at low pH. Yet, both the wild type IFITM3 and the 21 amino acid-deletion mutant inhibit HIV-1 replication equally well. Given the pH-independent nature of HIV-1 entry, our results suggest that IFITM3 can inhibit viruses that enter cells via different routes and that its N-terminal region is specifically required for controlling pH-dependent viruses.
PMID:
23055554
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23055554
The N-terminal region of IFITM3 modulates its antiviral activity through regulating IFITM3 cellular localization.
Jia R, Pan Q, Ding S, Rong L, Liu SL, Geng Y, Qiao W, Liang C.
Source
Key Laboratory of Molecular Microbiology and Biotechnology (Ministry of Education) and Key Laboratory of Microbial Functional Genomics (Tianjin), College of Life Sciences, Nankai University, Tianjin 300071, China.
Abstract
Interferon inducible transmembrane (IFITM) protein family members IFITM1, 2 and 3 restrict the infection of multiple enveloped viruses. Significant enrichment of a minor IFITM3 allele was recently reported in patients who were hospitalized for seasonal and 2009 H1N1 pandemic flu. This IFITM3 allele lacks the first amino-terminal 21 amino acids and is unable to inhibit influenza A virus. In this study, we find that deleting this 21-amino acid region relocates IFITM3 from the endosomal compartments to cell periphery. This finding likely underlies the lost inhibition of influenza A virus that completes its entry exclusively within endosomes at low pH. Yet, both the wild type IFITM3 and the 21 amino acid-deletion mutant inhibit HIV-1 replication equally well. Given the pH-independent nature of HIV-1 entry, our results suggest that IFITM3 can inhibit viruses that enter cells via different routes and that its N-terminal region is specifically required for controlling pH-dependent viruses.
PMID:
23055554
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23055554