The 1A protein of respiratory syncytial virus is an integral membrane protein present as multiple, structurally distinct species

Abstract

OLMSTED AND COLLINS protocols (3); the details of the DNA inserts and constructions will be described elsewhere. Antisera. A synthetic peptide, designated lA-CT, was constructed to contain a cysteine residue followed by the C-terminal 12 amino acids of the predicted full-length 1A protein (Fig. 1). By using conventional procedures, the peptide was synthesized on an automated synthesizer, desalted, linked to keyhole limpet hemocyanin via the cysteine residue with the cross linker m-maleimidobenzoyl N-hydroxysuccinimide ester, and used to prepare specific rabbit antiserum. The peptide lA-CT and specific antiserum were kindly provided by W. Lee Maloy (Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, Bethesda, Md.). F-specific antiserum was raised in rabbits immunized with immunoaffinity-purified F protein (39) and was the generous gift of Peter Paradiso and Steven Hildreth (Praxis Biologics, Rochester, N.Y.). Radiolabeling, immunoprecipitation, and gel electrophoresis. Monolayer cultures of CV-1 or HEp-2 cells were infected with 2 to 5 PFU of RSV or 10 PFU of vaccinia-lA virus per cell. Radiolabeling was initiated at 8 h postinfection for vaccinia-lA virus or at 18 h postinfection for RSV unless otherwise noted in the figure legends. Unless otherwise noted, labeling with [35S]methionine was at 100 pXCi/ml for 30

TGEV corona virus ORF4 encodes a membrane protein that is incorporated into virions

“…Small integral membrane proteins have been described in several other enveloped RNA viruses, including Sindbis and Semliki Forest togaviruses, influenza A and B viruses, Simian virus 5, and respiratory syncitial paramyxoviruses (Garoff et a/., 1980;Welch and Sefton, 1980;Lamb et al, 1985;Hiebert, 1985;Olmsted and Collins, 1989). The influenza virus M2 protein (15K) and the alphavirus 6K protein are both acylated, Nexo-Cendo transmembrane polypeptides.…”

Inhibition of the Human Respiratory Syncytial Virus Small Hydrophobic Protein and Structural Variations in a Bicelle Environment

“…In infected cells, most SH protein accumulates at the membranes of the Golgi complex, but it has also been detected in the endoplasmic reticulum and plasma membranes (14). During infection, the full-length unmodified form is the major species (15) although a truncated form (4.5 kDa) and glycosylated and phosphorylated forms have also been detected (16,17). SH protein has a single predicted ␣-helical transmembrane (TM) domain (15) which is highly conserved (18,19).…”

The Small Hydrophobic Protein of the Human Respiratory Syncytial Virus Forms Pentameric Ion Channels

“…During infection, SH protein has been shown to exist in several forms, e.g. full-length truncated protein (4.5 kDa), and post-translationally modified by glycosylation and phosphorylation (14,15), although the full-length unmodified form is the major species (10).…”