دورية أكاديمية

The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain.

التفاصيل البيبلوغرافية
العنوان: The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain.
المؤلفون: Tsai JC; Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia 19104, USA., Zelus BD, Holmes KV, Weiss SR
المصدر: Journal of virology [J Virol] 2003 Jan; Vol. 77 (2), pp. 841-50.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0113724 Publication Model: Print Cited Medium: Print ISSN: 0022-538X (Print) Linking ISSN: 0022538X NLM ISO Abbreviation: J Virol Subsets: MEDLINE
أسماء مطبوعة: Publication: Washington Dc : American Society For Microbiology
Original Publication: Baltimore, American Society for Microbiology.
مواضيع طبية MeSH: Antigens, CD/*metabolism , Antigens, Differentiation/*metabolism , Coronavirus/*metabolism , Membrane Glycoproteins/*metabolism , Viral Envelope Proteins/*metabolism, Animals ; Base Sequence ; Carcinoembryonic Antigen ; Cell Adhesion Molecules ; Cell Line ; Cricetinae ; DNA Primers ; Liposomes ; Membrane Glycoproteins/chemistry ; Mice ; Protein Binding ; Protein Conformation ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/chemistry
مستخلص: Using isogenic recombinant murine coronaviruses expressing wild-type murine hepatitis virus strain 4 (MHV-4) or MHV-A59 spike glycoproteins or chimeric MHV-4/MHV-A59 spike glycoproteins, we have demonstrated the biological functionality of the N-terminus of the spike, encompassing the receptor binding domain (RBD). We have used two assays, one an in vitro liposome binding assay and the other a tissue culture replication assay. The liposome binding assay shows that interaction of the receptor with spikes on virions at 37 degrees C causes a conformational change that makes the virions hydrophobic so that they bind to liposomes (B. D. Zelus, J. H. Schickli, D. M. Blau, S. R. Weiss, and K. V. Holmes, J. Virol. 77: 830-840, 2003). Recombinant viruses with spikes containing the RBD of either MHV-A59 or MHV-4 readily associated with liposomes at 37 degrees C in the presence of soluble mCEACAM1(a), except for S(4)R, which expresses the entire wild-type MHV-4 spike and associated only inefficiently with liposomes following incubation with soluble mCEACAM1(a). In contrast, soluble mCEACAM1(b) allowed viruses with the MHV-A59 RBD to associate with liposomes more efficiently than did viruses with the MHV-4 RBD. In the second assay, which requires virus entry and replication, all recombinant viruses replicated efficiently in BHK cells expressing mCEACAM1(a). In BHK cells expressing mCEACAM1(b), only viruses expressing chimeric spikes with the MHV-A59 RBD could replicate, while replication of viruses expressing chimeric spikes with the MHV-4 RBD was undetectable. Despite having the MHV-4 RBD, S(4)R replicated in BHK cells expressing mCEACAM1(b); this is most probably due to spread via CEACAM1 receptor-independent cell-to-cell fusion, an activity displayed only by S(4)R among the recombinant viruses studied here. These data suggest that the RBD domain and the rest of the spike must coevolve to optimize function in viral entry and spread.
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معلومات مُعتمدة: P01 NS030606 United States NS NINDS NIH HHS; T32 AI007325 United States AI NIAID NIH HHS; NS-21954 United States NS NINDS NIH HHS; AI-25231 United States AI NIAID NIH HHS; R01 AI025231 United States AI NIAID NIH HHS; T32-AI-07325 United States AI NIAID NIH HHS; NS-30606 United States NS NINDS NIH HHS
المشرفين على المادة: 0 (Antigens, CD)
0 (Antigens, Differentiation)
0 (CD66 antigens)
0 (Carcinoembryonic Antigen)
0 (Ceacam1 protein, mouse)
0 (Cell Adhesion Molecules)
0 (DNA Primers)
0 (Liposomes)
0 (Membrane Glycoproteins)
0 (Spike Glycoprotein, Coronavirus)
0 (Viral Envelope Proteins)
تواريخ الأحداث: Date Created: 20021228 Date Completed: 20030122 Latest Revision: 20190508
رمز التحديث: 20240627
مُعرف محوري في PubMed: PMC140794
DOI: 10.1128/jvi.77.2.841-850.2003
PMID: 12502800
قاعدة البيانات: MEDLINE
الوصف
تدمد:0022-538X
DOI:10.1128/jvi.77.2.841-850.2003