title: Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion.
abstract: The binding domains of four monoclonal antibodies (MAbs) specific for the M protein of the PUR46-MAD strain of transmissible gastroenteritis coronavirus (TGEV) have been located in the 46 carboxy-terminal amino acids of the protein by studying the binding of MAbs to recombinant M protein fragments. Immunoelectron microscopy using these MAbs demonstrated that in a significant proportion of the M protein molecules, the carboxy terminus is exposed on the external surface both in purified viruses and in nascent TGEV virions that recently exited infected swine testis cells. The same MAbs specifically neutralized the infectivity of the PUR46-MAD strain, indicating that the C-terminal domain of M protein is exposed on infectious viruses. This topology of TGEV M protein probably coexists with the structure currently described for the M protein of coronaviruses, which consists of an exposed amino terminus and an intravirion carboxy-terminal domain. The presence of a detectable number of M protein molecules with their carboxy termini exposed on the surface of the virion has relevance for viral function, since it has been shown that the carboxy terminus of M protein is immunodominant and that antibodies specific for this domain both neutralize TGEV and mediate the complement-dependent lysis of TGEV-infected cells.
authors.affiliation: Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
authors.forename: C
authors.initials: C
authors.lastname: Risco
authors.forename: I M
authors.initials: IM
authors.lastname: Antón
authors.forename: C
authors.initials: C
authors.lastname: Suñé
authors.forename: A M
authors.initials: AM
authors.lastname: Pedregosa
authors.forename: J M
authors.initials: JM
authors.lastname: Martín-Alonso
authors.forename: F
authors.initials: F
authors.lastname: Parra
authors.forename: J L
authors.initials: JL
authors.lastname: Carrascosa
authors.forename: L
authors.initials: L
authors.lastname: Enjuanes
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D000937:Antigen-Antibody Reactions; D000956:Antigens, Viral / Q000032:analysis; D002478:Cells, Cultured; D003001:Cloning, Molecular; D008297:Male; D051379:Mice / Q000276:immunology; D016253:Microscopy, Immunoelectron; D008961:Models, Structural; D009500:Neutralization Tests; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000737:chemistry / Q000276:immunology; D013552:Swine; D013737:Testis; D005760:Transmissible gastroenteritis virus / Q000378:metabolism* / Q000648:ultrastructure; D014763:Viral Matrix Proteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D014771:Virion / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D011993:Recombinant Fusion Proteins; D014763:Viral Matrix Proteins