Trimerisoituminen. Lähteitä.

 Etsin  trimerisoitumisen linkkejä.

Sars-23 virus koodaa S-proteiininsa monomeerina. Se trimerisotuu muotoon, josa se on S-piikki viruksen pinnassa . Sillä on lyhyt  transmembraaninen osa ja pieni intravirioninen osa. 

TIETYSTI  isäntäsolu värkk virukselle näitä trimeerejä jotenkin. Etsin ihmisen proteiineista trimerisoitumisesimerkkejä

 Heat stress proteins

https://www.jbc.org/article/S0021-9258(19)72901-9/pdf

 

. 2020 Dec;9(1):2663-2672.

doi: 10.1080/22221751.2020.1850183.

Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target

Cun Li  ^{1   2} , Hin Chu  ^{1   2} , Xiaojuan Liu  ² , Man Chun Chiu  ² , Xiaoyu Zhao  ² , Dong Wang  ² , Yuxuan Wei  ² , Yuxin Hou  ² , Huiping Shuai  ² , Jianpiao Cai  ² , Jasper Fuk-Woo Chan  ^{1   2   3} , Jie Zhou  ^{1   2} , Kwok Yung Yuen  ^{1   2   3}

Affiliations

• PMID: 33179566
• PMCID: PMC7751432
• DOI: 10.1080/22221751.2020.1850183

Free PMC article

Abstract

Rapid accumulation of viral proteins in host cells render viruses highly dependent on cellular chaperones including heat shock protein 90 (Hsp90). Three highly pathogenic human coronaviruses, including MERS-CoV, SARS-CoV and SARS-CoV-2, have emerged in the past 2 decades. However, there is no approved antiviral agent against these coronaviruses. We inspected the role of Hsp90 for coronavirus propagation. First, an Hsp90 inhibitor, 17-AAG, significantly suppressed MERS-CoV propagation in cell lines and physiological-relevant human intestinal organoids. Second, siRNA depletion of Hsp90β, but not Hsp90α, significantly restricted MERS-CoV replication and abolished virus spread. Third, Hsp90β interaction with MERS-CoV nucleoprotein (NP) was revealed in a co-immunoprecipitation assay. Hsp90β is required to maintain NP stability. Fourth, 17-AAG substantially inhibited the propagation of SARS-CoV and SARS-CoV-2. Collectively, Hsp90 is a host dependency factor for human coronavirus MERS-CoV, SARS-CoV and SARS-COV-2. Hsp90 inhibitors can be repurposed as a potent and broad-spectrum antiviral against human coronaviruses.

Keywords: Coronavirus; Hsp90β; SARS-CoV-2; nucleoprotein; viral replication. 

 

Ihmisen HSP proteiinit

 https://www.ebi.ac.uk/interpro/entry/InterPro/IPR001404/

 Description

Molecular chaperones, or heat shock proteins (Hsps) are ubiquitous proteins that act to maintain proper protein folding within the cell

^[1]. They assist in the folding of nascent polypeptide chains, and are also involved in the re-folding of denatured proteins following proteotoxic stress. As their name implies, the heat shock proteins were first identified as proteins that were up-regulated under conditions of elevated temperature. However, subsequent studies have shown that increased Hsp expression is induced by a variety of cellular stresses, including oxidative stress and inflammation. 

have been determined, and are categorized according to their molecular size (Hsp100, Hsp90, Hsp70, Hsp60, and the small Hsps). Hsps are involved in a variety of cellular processes that are ATP-dependent. These include: prevention of protein aggregation, protein degradation, protein trafficking, and maintenance of signalling proteins in a conformation that permits activation.

Hsp90 chaperones are unique in their ability to regulate a specific subset of cellular signalling proteins that have been implicated in disease processes, including intracellular protein kinases, steroid hormone receptors, and growth factor receptors

^[2]

.

 TRAF ja trimerisaatio  ihmisproteiinissa. Tästä seuraava otsikko.