دورية أكاديمية
The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain.
العنوان: | The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain. |
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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. |
References: | Virology. 1994 Apr;200(1):1-10. (PMID: 8128613) J Virol. 1998 Mar;72(3):1941-8. (PMID: 9499047) J Virol. 2000 Feb;74(3):1393-406. (PMID: 10627550) Virology. 2000 Jul 20;273(1):80-9. (PMID: 10891410) J Virol. 2000 Oct;74(19):9206-13. (PMID: 10982367) Virology. 2001 Jan 20;279(2):371-4. (PMID: 11162792) J Virol. 2001 Mar;75(6):2792-802. (PMID: 11222703) Exp Cell Res. 1999 Nov 1;252(2):243-9. (PMID: 11501563) J Neurovirol. 2001 Oct;7(5):421-31. (PMID: 11582514) Virology. 1995 Apr 1;208(1):67-74. (PMID: 11831732) J Virol. 2003 Jan;77(2):830-40. (PMID: 12502799) Arch Neurol. 1973 May;28(5):298-303. (PMID: 4348723) Neurology. 1984 May;34(5):597-603. (PMID: 6324031) J Virol. 1987 Jan;61(1):185-9. (PMID: 3023696) Proc Natl Acad Sci U S A. 1987 Sep;84(18):6567-71. (PMID: 2442761) Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2580-5. (PMID: 9482929) Virology. 1998 May 10;244(2):483-94. (PMID: 9601516) J Virol. 1998 Sep;72(9):7237-44. (PMID: 9696818) J Virol. 1998 Dec;72(12):9628-36. (PMID: 9811696) J Virol. 1999 Jan;73(1):638-49. (PMID: 9847369) J Virol. 1999 Sep;73(9):7607-18. (PMID: 10438851) J Virol. 1999 Sep;73(9):7752-60. (PMID: 10438865) J Virol. 1999 Oct;73(10):8152-9. (PMID: 10482565) Eur J Biochem. 1999 Sep;264(2):534-44. (PMID: 10491101) J Mol Biol. 1987 Aug 20;196(4):963-6. (PMID: 3681988) J Gen Virol. 1988 Dec;69 ( Pt 12):2939-52. (PMID: 3058868) Virology. 1989 Dec;173(2):664-73. (PMID: 2556846) J Virol. 1990 Jun;64(6):3051-5. (PMID: 1692350) Lab Invest. 1990 May;62(5):570-8. (PMID: 2160561) J Virol. 1991 Dec;65(12):6881-91. (PMID: 1719235) J Virol. 1992 Apr;66(4):1841-8. (PMID: 1312608) Nature. 1992 Jun 4;357(6377):417-20. (PMID: 1350661) Nature. 1992 Jun 4;357(6377):420-2. (PMID: 1350662) Virology. 1992 Nov;191(1):517-22. (PMID: 1413526) J Virol. 1992 Dec;66(12):6931-8. (PMID: 1279194) J Virol. 1992 Dec;66(12):7420-8. (PMID: 1279203) J Virol. 1993 Jan;67(1):1-8. (PMID: 8380065) J Gen Virol. 1993 Feb;74 ( Pt 2):183-91. (PMID: 8381459) J Virol. 1993 Mar;67(3):1185-94. (PMID: 7679743) Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1716-20. (PMID: 8383324) Virology. 1993 Apr;193(2):545-62. (PMID: 8460475) J Virol. 1993 Aug;67(8):4504-12. (PMID: 8392595) Brain Res Dev Brain Res. 1994 Mar 18;78(1):35-43. (PMID: 8004772) J Virol. 1994 Sep;68(9):5403-10. (PMID: 7520090) Lab Invest. 1995 Nov;73(5):615-27. (PMID: 7474935) J Virol. 1996 Dec;70(12):8669-74. (PMID: 8970993) J Virol. 1997 Feb;71(2):1688-91. (PMID: 8995701) J Virol. 1997 Mar;71(3):1946-55. (PMID: 9032326) J Virol. 1997 Apr;71(4):3129-37. (PMID: 9060676) Virology. 1997 Mar 17;229(2):336-48. (PMID: 9126247) J Virol. 1997 Jul;71(7):5148-60. (PMID: 9188582) J Virol. 1997 Nov;71(11):8860-3. (PMID: 9343248) J Virol. 1997 Dec;71(12):9024-31. (PMID: 9371559) J Cell Biol. 1997 Dec 15;139(6):1455-64. (PMID: 9396751) J Virol. 1994 Jul;68(7):4525-37. (PMID: 8207827) |
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 |
تدمد: | 0022-538X |
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DOI: | 10.1128/jvi.77.2.841-850.2003 |