GSBS Student Publications
Title
Translation and membrane insertion of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus
GSBS Program
Not applicable
Publication Date
1987-04-01
UMMS Affiliation
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology; Department of Molecular Genetics and Microbiology
Document Type
Article
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
The hemagglutinin-neuraminidase (HN) protein of paramyxoviruses is likely in the unusual class of glycoproteins with the amino terminus cytoplasmic and the carboxy terminus lumenal or external to the cell. The properties of the membrane insertion of the HN protein of Newcastle disease virus, a prototype paramyxovirus, were explored in wheat germ extracts containing microsomal membranes. HN protein was inserted into membranes cotranslationally, resulting in a glycosylated protein completely resistant to trypsin and proteinase K digestion. No detectable posttranslation insertion occurred. Insertion required signal recognition particle. Signal recognition particle in the absence of membranes inhibited HN protein synthesis. Comparisons of the trypsin digestion products of the HN protein made in the cell-free system with newly synthesized HN protein from infected cells showed that the cell-free product was in a conformation different from that of the pulse-labeled protein in infected cells. First, trypsin digestion of intact membranes from infected cells reduced the size of the 74,000-dalton HN protein by approximately 1,000 daltons, whereas trypsin digestion of HN protein made in the cell-free system had no effect on the size of the protein. Second, trypsin digestion of Triton X-100-permeabilized membranes isolated from infected cells resulted in a 67,000-dalton trypsin resistant HN protein fragment. A trypsin-resistant core of comparable size was not present in the digestion products of in-vitro-synthesized HN protein. Evidence is presented that the newly synthesized HN protein in infected cels contain intramolecular disulfide bonds not present in the cell-free product.
DOI of Published Version
10.1128/MCB.7.4.1386
Source
Mol Cell Biol. 1987 Apr;7(4):1386-92.
Journal/Book/Conference Title
Molecular and cellular biology
Related Resources
PubMed ID
3600630
Repository Citation
Wilson CA, Gilmore R, Morrison TG. (1987). Translation and membrane insertion of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus. GSBS Student Publications. https://doi.org/10.1128/MCB.7.4.1386. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/935