FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2766504265> ?p ?o ?g. }

• W2766504265 abstract "ABSTRACT Coronaviruses recently emerged as major human pathogens causing outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome. They utilize the spike (S) glycoprotein anchored in the viral envelope to mediate host attachment and fusion of the viral and cellular membranes to initiate infection. The S protein is a major determinant of the zoonotic potential of coronaviruses and is also the main target of the host humoral immune response. We report here the 3.5-Å-resolution cryo-electron microscopy structure of the S glycoprotein trimer from the pathogenic porcine deltacoronavirus (PDCoV), which belongs to the recently identified Deltacoronavirus genus. Structural and glycoproteomics data indicate that the glycans of PDCoV S are topologically conserved compared with the human respiratory coronavirus NL63 S, resulting in similar surface areas being shielded from neutralizing antibodies and implying that both viruses are under comparable immune pressure in their respective hosts. The structure further reveals a shortened S 2 ′ activation loop, containing a reduced number of basic amino acids, which participates in rendering the spike largely protease resistant. This property distinguishes PDCoV S from recently characterized betacoronavirus S proteins and suggests that the S protein of enterotropic PDCoV has evolved to tolerate the protease-rich environment of the small intestine and to fine-tune its fusion activation to avoid premature triggering and reduction of infectivity. IMPORTANCE Coronaviruses use transmembrane S glycoprotein trimers to promote host attachment and fusion of the viral and cellular membranes. We determined a near-atomic-resolution cryo-electron microscopy structure of the S ectodomain trimer from the pathogenic PDCoV, which is responsible for diarrhea in piglets and has had devastating consequences for the swine industry worldwide. Structural and glycoproteomics data reveal that PDCoV S is decorated with 78 N-linked glycans obstructing the protein surface to limit accessibility to neutralizing antibodies in a way reminiscent of what has recently been described for a human respiratory coronavirus. PDCoV S is largely protease resistant, which distinguishes it from most other characterized coronavirus S glycoproteins and suggests that enteric coronaviruses have evolved to fine-tune fusion activation in the protease-rich environment of the small intestine of infected hosts." @default.
• W2766504265 created "2017-11-10" @default.
• W2766504265 creator A5006351471 @default.
• W2766504265 creator A5006936042 @default.
• W2766504265 creator A5013854148 @default.
• W2766504265 creator A5021781776 @default.
• W2766504265 creator A5028725593 @default.
• W2766504265 creator A5034137050 @default.
• W2766504265 creator A5050510032 @default.
• W2766504265 creator A5080132990 @default.
• W2766504265 creator A5083617730 @default.
• W2766504265 creator A5085406779 @default.
• W2766504265 date "2018-02-15" @default.
• W2766504265 modified "2023-10-18" @default.
• W2766504265 title "Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections" @default.
• W2766504265 cites W103562566 @default.
• W2766504265 cites W1539248632 @default.
• W2766504265 cites W1860515130 @default.
• W2766504265 cites W1965411122 @default.
• W2766504265 cites W1965531501 @default.
• W2766504265 cites W1967608615 @default.
• W2766504265 cites W1972940026 @default.
• W2766504265 cites W1973757205 @default.
• W2766504265 cites W1974355337 @default.
• W2766504265 cites W1975490802 @default.
• W2766504265 cites W1982533785 @default.
• W2766504265 cites W1989750370 @default.
• W2766504265 cites W1993577573 @default.
• W2766504265 cites W1994915168 @default.
• W2766504265 cites W2025977980 @default.
• W2766504265 cites W2028470175 @default.
• W2766504265 cites W2036949898 @default.
• W2766504265 cites W2054757078 @default.
• W2766504265 cites W2054770020 @default.
• W2766504265 cites W2064140868 @default.
• W2766504265 cites W2064350446 @default.
• W2766504265 cites W2075824676 @default.
• W2766504265 cites W2077524199 @default.
• W2766504265 cites W2085887280 @default.
• W2766504265 cites W2086549128 @default.
• W2766504265 cites W2097604487 @default.
• W2766504265 cites W2103747393 @default.
• W2766504265 cites W2104234755 @default.
• W2766504265 cites W2105637133 @default.
• W2766504265 cites W2107520340 @default.
• W2766504265 cites W2115137014 @default.
• W2766504265 cites W2120967846 @default.
• W2766504265 cites W2121009566 @default.
• W2766504265 cites W2122276188 @default.
• W2766504265 cites W2124026197 @default.
• W2766504265 cites W2124153977 @default.
• W2766504265 cites W2129508783 @default.
• W2766504265 cites W2130255548 @default.
• W2766504265 cites W2134061616 @default.
• W2766504265 cites W2134972446 @default.
• W2766504265 cites W2142157385 @default.
• W2766504265 cites W2142161929 @default.
• W2766504265 cites W2143901293 @default.
• W2766504265 cites W2146064229 @default.
• W2766504265 cites W2146242600 @default.
• W2766504265 cites W2146374988 @default.
• W2766504265 cites W2149561246 @default.
• W2766504265 cites W2152562710 @default.
• W2766504265 cites W2154026160 @default.
• W2766504265 cites W2154359066 @default.
• W2766504265 cites W2154714625 @default.
• W2766504265 cites W2154988647 @default.
• W2766504265 cites W2155728582 @default.
• W2766504265 cites W2158922816 @default.
• W2766504265 cites W2161328280 @default.
• W2766504265 cites W2172295047 @default.
• W2766504265 cites W2217313808 @default.
• W2766504265 cites W2255243349 @default.
• W2766504265 cites W2256708510 @default.
• W2766504265 cites W2271364844 @default.
• W2766504265 cites W2285594236 @default.
• W2766504265 cites W2292700442 @default.
• W2766504265 cites W2298153446 @default.
• W2766504265 cites W2336507460 @default.
• W2766504265 cites W2432427150 @default.
• W2766504265 cites W2520033800 @default.
• W2766504265 cites W2521026695 @default.
• W2766504265 cites W2527400873 @default.
• W2766504265 cites W2564443324 @default.
• W2766504265 cites W2593511418 @default.
• W2766504265 cites W2606148195 @default.
• W2766504265 cites W2750464792 @default.
• W2766504265 cites W2762161295 @default.
• W2766504265 cites W2950967305 @default.
• W2766504265 cites W2951664934 @default.
• W2766504265 cites W2953320394 @default.
• W2766504265 doi "https://doi.org/10.1128/jvi.01628-17" @default.
• W2766504265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5790929" @default.
• W2766504265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29093093" @default.
• W2766504265 hasPublicationYear "2018" @default.
• W2766504265 type Work @default.
• W2766504265 sameAs 2766504265 @default.
• W2766504265 citedByCount "115" @default.
• W2766504265 countsByYear W27665042652018 @default.
• W2766504265 countsByYear W27665042652019 @default.

• next