Structure of semliki forest virus core protein

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Abstract Alphaviruses are enveloped, insect-borne viruses, which contains a positive-sense RNA genome. The protein capsid is surrounded by a lipid membrane, which is penetrated by glycoprotein spikes. SCP is a serine proteinase which cleaves itself from a polyprotein. Similar to SCP, autocatalysis is inhibited in SFCP after cleavage of the polyprotein by leaving the carboxy-terminal tryptophan in the specificity pocket.

While monomers A and B make a tail-to-tail dimer contact, monomers B and C make a head-to-head dimer contact. A hydrophobic pocket on the surface of the capsid protein, the proposed site of binding of the E2 glycoprotein, has large conformational differences with respect to SCP and, in contrast to SCP, is found devoid of bound peptide. This suggests, by comparison with SCP, that E2 binding to cores causes major conformational changes, including the burial of Tyr, which would stabilize the intact virus on budding from an infected cell.

The head-to-tail contacts found in the pentameric and hexameric associations within the virion utilize in the same monomer surface regions as found in the crystalline dimer interfaces. Full text links Read article at publisher's site DOI : 3.

References Articles referenced by this article 43 The alphaviruses: gene expression, replication, and evolution. Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Nucleocapsid and glycoprotein organization in an enveloped virus.

Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease. Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease.

Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. The structure determination of Sindbis virus core protein using isomorphous replacement and molecular replacement averaging between two crystal forms. Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease.

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Data Data that cites the article This data has been provided by curated databases and other sources that have cited the article. Protein Families. Protein Interactions. Protein Structures 2. View structure. Web of Science. Let us know here. System error. Please try again! How was the reading experience on this article?

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Thank you for submitting a report! Submitting a report will send us an email through our customer support system. Submit report Close. CO;2-G Publisher site 3. Journal Proteins: Structure Function and Bioinformatics — Wiley Published: Mar 1, Keywords: alphavirus structure; Semliki Forest virus capsid protein; autocatalysis; capsid assembly; conformational changes.

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Copyright notice. This article has been cited by other articles in PMC. Abstract Semlike forest virus capsid protein cosedimented with the large ribosomal subunit at 60S in sucrose gradients after treatment of cytoplasm from infected cells with Triton X and EDTA. Images in this article Image on p. Image on p.

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