title: The minor receptor group of human rhinovirus (HRV) includes HRV23 and HRV25, but the presence of a lysine in the VP1 HI loop is not sufficient for receptor binding.
abstract: Like all 10 minor receptor group human rhinoviruses (HRVs), HRV23 and HRV25, previously classified as major group viruses, are neutralized by maltose binding protein (MBP)-V33333 (a soluble recombinant concatemer of five copies of repeat 3 of the very-low-density lipoprotein receptor fused to MBP), bind to low-density lipoprotein receptor in virus overlay blots, and replicate in intercellular adhesion molecule 1 (ICAM-1)-negative COS-7 cells. From phylogenetic analysis of capsid protein VP1-coding sequences, they are also known to cluster together with other minor group strains. Therefore, they belong to the minor group; there are now 12 minor group and 87 major group HRV serotypes. Sequence comparison of the VP1 capsid proteins of all HRVs revealed that the lysine in the HI loop, strictly conserved in the 12 minor group HRVs, is also present in 9 major group serotypes that are neutralized by soluble ICAM-1. Despite the presence of this lysine, they are not neutralized by MBP-V33333 and fail to replicate in COS-7 cells and in HeLa cells in the presence of an ICAM-1-blocking antibody. These nine serotypes are therefore "true" major group viruses.
authors.affiliation: Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr Gasse 9/3, A-1030 Vienna, Austria.
authors.forename: Marketa
authors.initials: M
authors.lastname: Vlasak
authors.forename: Merja
authors.initials: M
authors.lastname: Roivainen
authors.forename: Manuela
authors.initials: M
authors.lastname: Reithmayer
authors.forename: Irene
authors.initials: I
authors.lastname: Goesler
authors.forename: Pia
authors.initials: P
authors.lastname: Laine
authors.forename: Luc
authors.initials: L
authors.lastname: Snyers
authors.forename: Tapani
authors.initials: T
authors.lastname: Hovi
authors.forename: Dieter
authors.initials: D
authors.lastname: Blaas
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D002352:Carrier Proteins / Q000378:metabolism; D002522:Chlorocebus aethiops; D006367:HeLa Cells; D006801:Humans; D008239:Lysine; D058619:Maltose-Binding Proteins; D008969:Molecular Sequence Data; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D011973:Receptors, LDL / Q000378:metabolism; D012229:Rhinovirus / Q000145:classification / Q000378:metabolism* / Q000472:pathogenicity; D016415:Sequence Alignment; D012703:Serotyping; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D011973:Receptors, LDL; D014157:Transcription Factors; D014764:Viral Proteins; C074995:viral protein 1, rhinovirus; D008239:Lysine