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J Gen Virol 74 (1993), 1445-1450; DOI 10.1099/0022-1317-74-7-1445
© 1993 Society for General Microbiology
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Membrane orientation and oligomerization of the small hydrophobic protein of human respiratory syncytial virus

Peter L. Collins and Geneviève Mottet{dagger}

Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Building 7, Room 100, Bethesda, Maryland 20892, U.S.A.

Previous work has demonstrated that the small hydrophobic (SH) protein of human respiratory syncytial virus (RSV) A2 strain is a 64 amino acid integral membrane protein that accumulates intracellularly as an unglycosylated major species (SH0), a minor species truncated at the amino terminus and two N-glycosylated species one of which contains a further addition of polylactosamine. In this study, the membrane orientation of SH0 was mapped by trypsinization of intact RSV-infected cells followed by washout, lysis and immunoprecipitation of protected fragments with antisera specific for the protein termini. This showed that the C terminus is extracellular and the SH protein was not detectably palmitylated. Analysis of the SH protein by sedimentation on sucrose gradients showed that it rapidly assembles into a homo-oligomer that cosediments with the F protein tetramer. Interestingly, all forms of the SH protein were found in the oligomeric fraction. Chemical cross-linking generated species which appeared to represent dimers, trimers, tetramers and pentamers as well as a minor species of 180K which might correspond to the oligomeric form detected by sucrose gradient sedimentation.

{dagger} Present address: Department of Microbiology, CMU, University of Geneva, Geneva, Switzerland.

Received 6 January 1992; accepted 1 March 1993.


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