Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu

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作   者：

Fapohunda, Oluwaseun;  Wang, Zhihan;  Pham, Hieu;  Taylor, Michael T.;  Kloss, Brian;  Townsend, Julia A.;  Park, Sang Ho;  Opella, Stanley;  Aspinwall, Craig A.;  Marty, Michael T.; 

作者机构：

University of California San Diego Department of Chemistry and Biochemistry;  The University of Arizona College of Medicine Tucson;  Univ Arizona; 

关键词：

3-DIMENSIONAL STRUCTURE;  MYRISTOYLATION;  NMR;  IMMUNODEFICIENCY-VIRUS TYPE-1;  ION-CHANNEL;  VIROPORINS STRUCTURE;  TRANSMEMBRANE DOMAIN;  MEMBRANE-PROTEIN;  IONIZATION;  MASS-SPECTROMETRY; 

期刊名称：

Biochemistry

i s s n：

0006-2960

年卷期：

2024 年 63 卷 3 期

页   码：

241-250

页   码：

摘   要：

Viroporins constitute a class of viral membrane proteins with diverse roles in the viral life cycle. They can self-assemble and form pores within the bilayer that transport substrates, such as ions and genetic material, that are critical to the viral infection cycle. However, there is little known about the oligomeric state of most viroporins. Here, we use native mass spectrometry in detergent micelles to uncover the patterns of oligomerization of the full-length SARS-CoV-2 envelope (E) protein, poliovirus VP4, and HIV Vpu. Our data suggest that the E protein is a specific dimer, VP4 is exclusively monomeric, and Vpu assembles into a polydisperse mixture of oligomers under these conditions. Overall, these results revealed the diversity in the oligomerization of viroporins, which has implications for the mechanisms of their biological functions as well as their potential as therapeutic targets.