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Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.
J Biol Chem. 2010 Apr 23; 285(17):12862-72.JB

Abstract

Coronavirus membrane (M) protein can form virus-like particles (VLPs) when coexpressed with nucleocapsid (N) or envelope (E) proteins, suggesting a pivotal role for M in virion assembly. Here we demonstrate the self-assembly and release of severe acute respiratory syndrome coronavirus (SARS-CoV) M protein in medium in the form of membrane-enveloped vesicles with densities lower than those of VLPs formed by M plus N. Although efficient N-N interactions require the presence of RNA, we found that M-M interactions were RNA-independent. SARS-CoV M was observed in both the Golgi area and plasma membranes of a variety of cells. Blocking M glycosylation does not appear to significantly affect M plasma membrane labeling intensity, M-containing vesicle release, or VLP formation. Results from a genetic analysis indicate involvement of the third transmembrane domain of M in plasma membrane-targeting signal. Fusion proteins containing M amino-terminal 50 residues encompassing the first transmembrane domain were found to be sufficient for membrane binding, multimerization, and Golgi retention. Surprisingly, we found that fusion proteins lacking all three transmembrane domains were still capable of membrane binding, Golgi retention, and interacting with M. The data suggest that multiple SARS-CoV M regions are involved in M self-assembly and subcellular localization.

Authors+Show Affiliations

Department of Medical Research and Education, Taipei Veterans General Hospital, Taiwan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20154085

Citation

Tseng, Ying-Tzu, et al. "Self-assembly of Severe Acute Respiratory Syndrome Coronavirus Membrane Protein." The Journal of Biological Chemistry, vol. 285, no. 17, 2010, pp. 12862-72.
Tseng YT, Wang SM, Huang KJ, et al. Self-assembly of severe acute respiratory syndrome coronavirus membrane protein. J Biol Chem. 2010;285(17):12862-72.
Tseng, Y. T., Wang, S. M., Huang, K. J., Lee, A. I., Chiang, C. C., & Wang, C. T. (2010). Self-assembly of severe acute respiratory syndrome coronavirus membrane protein. The Journal of Biological Chemistry, 285(17), 12862-72. https://doi.org/10.1074/jbc.M109.030270
Tseng YT, et al. Self-assembly of Severe Acute Respiratory Syndrome Coronavirus Membrane Protein. J Biol Chem. 2010 Apr 23;285(17):12862-72. PubMed PMID: 20154085.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Self-assembly of severe acute respiratory syndrome coronavirus membrane protein. AU - Tseng,Ying-Tzu, AU - Wang,Shiu-Mei, AU - Huang,Kuo-Jung, AU - Lee,Amber I-Ru, AU - Chiang,Chien-Cheng, AU - Wang,Chin-Tien, Y1 - 2010/02/12/ PY - 2010/2/16/entrez PY - 2010/2/16/pubmed PY - 2010/5/21/medline SP - 12862 EP - 72 JF - The Journal of biological chemistry JO - J Biol Chem VL - 285 IS - 17 N2 - Coronavirus membrane (M) protein can form virus-like particles (VLPs) when coexpressed with nucleocapsid (N) or envelope (E) proteins, suggesting a pivotal role for M in virion assembly. Here we demonstrate the self-assembly and release of severe acute respiratory syndrome coronavirus (SARS-CoV) M protein in medium in the form of membrane-enveloped vesicles with densities lower than those of VLPs formed by M plus N. Although efficient N-N interactions require the presence of RNA, we found that M-M interactions were RNA-independent. SARS-CoV M was observed in both the Golgi area and plasma membranes of a variety of cells. Blocking M glycosylation does not appear to significantly affect M plasma membrane labeling intensity, M-containing vesicle release, or VLP formation. Results from a genetic analysis indicate involvement of the third transmembrane domain of M in plasma membrane-targeting signal. Fusion proteins containing M amino-terminal 50 residues encompassing the first transmembrane domain were found to be sufficient for membrane binding, multimerization, and Golgi retention. Surprisingly, we found that fusion proteins lacking all three transmembrane domains were still capable of membrane binding, Golgi retention, and interacting with M. The data suggest that multiple SARS-CoV M regions are involved in M self-assembly and subcellular localization. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/20154085/Self_assembly_of_severe_acute_respiratory_syndrome_coronavirus_membrane_protein_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)55066-7 DB - PRIME DP - Unbound Medicine ER -