FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2801478799> ?p ?o ?g. }

• W2801478799 endingPage "9944" @default.
• W2801478799 startingPage "9937" @default.
• W2801478799 abstract "Many enveloped viruses enter cells through the endocytic network, from which they must subsequently escape through fusion of viral and endosomal membranes. This membrane fusion is mediated by virus-encoded spikes that respond to the dynamic endosomal environment, which triggers conformational changes in the spikes that initiate the fusion process. Several fusion triggers have been identified and include pH, membrane composition, and endosome-resident proteins, and these cues dictate when and where viral fusion occurs. We recently reported that infection with an enveloped bunyavirus requires elevated potassium ion concentrations [K+], controlled by cellular K+ channels, that are encountered during viral transit through maturing endosomes. Here we reveal the molecular basis for the K+ requirement of bunyaviruses through the first direct visualization of a member of the Nairoviridae family, namely Hazara virus (HAZV), using cryo-EM. Using cryo-electron tomography, we observed HAZV spike glycoproteins within infectious HAZV particles exposed to both high and low [K+], which showed that exposure to K+ alone results in dramatic changes to the ultrastructural architecture of the virion surface. In low [K+], the spikes adopted a compact conformation arranged in locally ordered arrays, whereas, following exposure to high [K+], the spikes became extended, and spike–membrane interactions were observed. Viruses exposed to high [K+] also displayed enhanced infectivity, thus identifying K+ as a newly defined trigger that helps promote viral infection. Finally, we confirmed that K+ channel blockers are inhibitory to HAZV infection, highlighting the potential of K+ channels as anti-bunyavirus targets. Many enveloped viruses enter cells through the endocytic network, from which they must subsequently escape through fusion of viral and endosomal membranes. This membrane fusion is mediated by virus-encoded spikes that respond to the dynamic endosomal environment, which triggers conformational changes in the spikes that initiate the fusion process. Several fusion triggers have been identified and include pH, membrane composition, and endosome-resident proteins, and these cues dictate when and where viral fusion occurs. We recently reported that infection with an enveloped bunyavirus requires elevated potassium ion concentrations [K+], controlled by cellular K+ channels, that are encountered during viral transit through maturing endosomes. Here we reveal the molecular basis for the K+ requirement of bunyaviruses through the first direct visualization of a member of the Nairoviridae family, namely Hazara virus (HAZV), using cryo-EM. Using cryo-electron tomography, we observed HAZV spike glycoproteins within infectious HAZV particles exposed to both high and low [K+], which showed that exposure to K+ alone results in dramatic changes to the ultrastructural architecture of the virion surface. In low [K+], the spikes adopted a compact conformation arranged in locally ordered arrays, whereas, following exposure to high [K+], the spikes became extended, and spike–membrane interactions were observed. Viruses exposed to high [K+] also displayed enhanced infectivity, thus identifying K+ as a newly defined trigger that helps promote viral infection. Finally, we confirmed that K+ channel blockers are inhibitory to HAZV infection, highlighting the potential of K+ channels as anti-bunyavirus targets. Correction: Potassium is a trigger for conformational change in the fusion spike of an enveloped RNA virus.Journal of Biological ChemistryVol. 294Issue 7PreviewDrs. Fontana, Mankouri, and Barr should all have been listed as corresponding authors. Dr. Fontana's contact information is as follows: Tel.: 44-113-3434170; E-mail: [email protected] . Dr. Mankouri's contact information is as follows: Tel.: 44-113-3435646; E-mail: [email protected] . Full-Text PDF Open Access" @default.
• W2801478799 created "2018-05-17" @default.
• W2801478799 creator A5026573897 @default.
• W2801478799 creator A5028489397 @default.
• W2801478799 creator A5033909787 @default.
• W2801478799 creator A5037719383 @default.
• W2801478799 creator A5058186910 @default.
• W2801478799 creator A5061079514 @default.
• W2801478799 creator A5063711068 @default.
• W2801478799 creator A5078339069 @default.
• W2801478799 date "2018-06-01" @default.
• W2801478799 modified "2023-10-16" @default.
• W2801478799 title "Potassium is a trigger for conformational change in the fusion spike of an enveloped RNA virus" @default.
• W2801478799 cites W1541543918 @default.
• W2801478799 cites W1883862591 @default.
• W2801478799 cites W1963820178 @default.
• W2801478799 cites W1965772211 @default.
• W2801478799 cites W1968120157 @default.
• W2801478799 cites W1979711577 @default.
• W2801478799 cites W2002391464 @default.
• W2801478799 cites W2007322316 @default.
• W2801478799 cites W2028605946 @default.
• W2801478799 cites W2032146255 @default.
• W2801478799 cites W2036574626 @default.
• W2801478799 cites W2041093934 @default.
• W2801478799 cites W2044073966 @default.
• W2801478799 cites W2045649879 @default.
• W2801478799 cites W2069701880 @default.
• W2801478799 cites W2072897393 @default.
• W2801478799 cites W2089521177 @default.
• W2801478799 cites W2104130324 @default.
• W2801478799 cites W2106538910 @default.
• W2801478799 cites W2111094049 @default.
• W2801478799 cites W2118512554 @default.
• W2801478799 cites W2132629607 @default.
• W2801478799 cites W2134183665 @default.
• W2801478799 cites W2134855545 @default.
• W2801478799 cites W2147443197 @default.
• W2801478799 cites W2160589638 @default.
• W2801478799 cites W2167644802 @default.
• W2801478799 cites W2170933363 @default.
• W2801478799 cites W2204843529 @default.
• W2801478799 cites W2211940791 @default.
• W2801478799 cites W2256042984 @default.
• W2801478799 cites W2343619545 @default.
• W2801478799 cites W2469012076 @default.
• W2801478799 cites W2487704570 @default.
• W2801478799 cites W2543812999 @default.
• W2801478799 cites W2546281209 @default.
• W2801478799 cites W2766897017 @default.
• W2801478799 cites W2784113094 @default.
• W2801478799 cites W2787631224 @default.
• W2801478799 cites W2912229433 @default.
• W2801478799 cites W2950967305 @default.
• W2801478799 cites W307221082 @default.
• W2801478799 cites W4235010090 @default.
• W2801478799 cites W4235692674 @default.
• W2801478799 doi "https://doi.org/10.1074/jbc.ra118.002494" @default.
• W2801478799 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6028977" @default.
• W2801478799 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29678879" @default.
• W2801478799 hasPublicationYear "2018" @default.
• W2801478799 type Work @default.
• W2801478799 sameAs 2801478799 @default.
• W2801478799 citedByCount "31" @default.
• W2801478799 countsByYear W28014787992019 @default.
• W2801478799 countsByYear W28014787992020 @default.
• W2801478799 countsByYear W28014787992021 @default.
• W2801478799 countsByYear W28014787992022 @default.
• W2801478799 countsByYear W28014787992023 @default.
• W2801478799 crossrefType "journal-article" @default.
• W2801478799 hasAuthorship W2801478799A5026573897 @default.
• W2801478799 hasAuthorship W2801478799A5028489397 @default.
• W2801478799 hasAuthorship W2801478799A5033909787 @default.
• W2801478799 hasAuthorship W2801478799A5037719383 @default.
• W2801478799 hasAuthorship W2801478799A5058186910 @default.
• W2801478799 hasAuthorship W2801478799A5061079514 @default.
• W2801478799 hasAuthorship W2801478799A5063711068 @default.
• W2801478799 hasAuthorship W2801478799A5078339069 @default.
• W2801478799 hasBestOaLocation W28014787991 @default.
• W2801478799 hasConcept C102747710 @default.
• W2801478799 hasConcept C103038307 @default.
• W2801478799 hasConcept C106358424 @default.
• W2801478799 hasConcept C12554922 @default.
• W2801478799 hasConcept C140704245 @default.
• W2801478799 hasConcept C1491633281 @default.
• W2801478799 hasConcept C159047783 @default.
• W2801478799 hasConcept C202878990 @default.
• W2801478799 hasConcept C2522874641 @default.
• W2801478799 hasConcept C28005876 @default.
• W2801478799 hasConcept C2909404852 @default.
• W2801478799 hasConcept C55493867 @default.
• W2801478799 hasConcept C58475186 @default.
• W2801478799 hasConcept C79747257 @default.
• W2801478799 hasConcept C79879829 @default.
• W2801478799 hasConcept C86803240 @default.
• W2801478799 hasConcept C95444343 @default.
• W2801478799 hasConcept C97380033 @default.
• W2801478799 hasConceptScore W2801478799C102747710 @default.

• next