Home LiteratureArticle Details
PMID: 821054 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Enveloped virus acquires membrane defect when passaged in fibroblasts from I-cell disease patients.

Sly WS, Lagwinska E, Schlesinger S

Abstract

Sindbis virus obtained after passage on human fibroblasts from patients with I-cell disease (mucolipidosis II) and called I-cell virus differed from Sindbis virus obtained from chick fibroblasts or from normal human fibroblasts in two ways: (1) The I-cell virus was extremely unstable to freezing and thawing, (2) The I-cell virus showed greatly exaggerated sensitivity to inactivation by Triton X-100. Sindbis virus from fibroblasts from two patients with mucolipidosis III, a milder form of I-cell disease, showed similar, though milder, freeze-sensitivity. When freeze-sensitive I-cell virus was passaged once in mouse L-cells or normal human fibroblasts, the virus was no longer abnormal. The viral glycoproteins of I-cell virus were not distinguishable from viral glycoproteins of controls by sodium dodecyl sulfate gel electrophoresis. Gel filtration of the glycopeptides suggested small differences in two of the four glycopeptides. These findings indicate that Sindbis virus is phenotypically altered when grown on I-cell fibroblasts. These alterations must be attributed to viral envelope components derived from the host plasma membrane (membrane lipids) or to alterations in viral envelope glycoproteins. In either case, the alterations appear related to the genetic defect in I-cell fibroblasts. From these results it is clear that enveloped viruses can be useful to demonstrate and to analyze membrane defects in certain human diseases. The phenotypically altered viruses may, in turn, provide probes for studying the functional relationships of virus membrane components.

MeSH Terms
Cell Membrane/pathology Fibroblasts/pathology Freezing Glucuronidase/deficiency Glycoproteins/analysis Humans Lipid Metabolism, Inborn Errors/pathology Mucopolysaccharidosis I/pathology Mucopolysaccharidosis II/pathology Phenotype Polyethylene Glycols/pharmacology Sindbis Virus/drug effects,growth & development,ultrastructure Viral Proteins/analysis
Chemicals
Glycoproteins Viral Proteins Polyethylene Glycols Glucuronidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sly W S
Lagwinska E
Schlesinger S
References (17)
17 references, click to expand
  1. Growth of enveloped RNA viruses in a line of chinese hamster ovary cells with deficient N-acetylglucosaminyltransferase activity.
    J Virol. 1975 Jan;17(1):239-46 PMID: 173886
  2. Roentgen findings in mucolipidosis III (Pseudo-Hurler polydystrophy).
    Radiology. 1973 Jan;106(1):153-60 PMID: 4264747
  3. I-cell disease: a clinical picture.
    J Pediatr. 1971 Sep;79(3):360-5 PMID: 4327936
  4. A hypothesis for I-cell disease: defective hydrolases that do not enter lysosomes.
    Biochem Biophys Res Commun. 1972 Nov 15;49(4):992-9 PMID: 4345092
  5. Studies on the pathogenetic mechanism of I-cell disease in cultured fibroblasts.
    Pediatr Res. 1974 Nov;8(11):865-9 PMID: 4374680
  6. Formation of Sindbis virus proteins: identification of a precursor for one of the envelope proteins.
    J Virol. 1972 Nov;10(5):925-32 PMID: 4673887
  7. Glycoproteins of Sindbis virus: priliminary characterization of the oligosaccharides.
    J Virol. 1974 Sep;14(3):522-30 PMID: 4852175
  8. Isolation of a Sindbis virus variant by passage on mouse plasmacytoma cells.
    J Virol. 1975 Apr;15(4):1037-41 PMID: 1167912
  9. Mucolipidosis 3 (pseudo-Hurler polydystrophy): cytological and ultrastructural observations of cultured fibroblast cells.
    Clin Genet. 1973;4(5):388-97 PMID: 4201594
  10. Genetic heterogeneity in multiple lysosomal hydrolase deficiency.
    J Pediatr. 1974 Aug;85(2):192-8 PMID: 4276418
  11. Clinical, biochemical, and ultrastructural studies in a case of chondrodystrophy presenting the I-cell phenotype in tissue culture.
    J Pediatr. 1971 Sep;79(3):366-78 PMID: 4327937
  12. "I-cell" disease: leakage of lysosomal enzymes into extracellular fluids.
    N Engl J Med. 1971 Nov 4;285(19):1090-1 PMID: 4328711
  13. A recognition marker required for uptake of a lysosomal enzyme by cultured fibroblasts.
    Biochem Biophys Res Commun. 1974 Mar 15;57(1):55-61 PMID: 4364008
  14. The glycolipids and phospholipids of Sindbis virus and their relation to the lipids of the host cell plasma membrane.
    Virology. 1974 Oct;61(2):602-8 PMID: 4472788
  15. Structural proteins of lactic dehydrogenase virus.
    Virology. 1973 Sep;55(1):211-7 PMID: 4738049
  16. Kinetics of incorporation of structural proteins into Sindbis virions.
    J Virol. 1969 Apr;3(4):369-75 PMID: 5771964
  17. Mutant enzymatic and cytological phenotypes in cultured human fibroblasts.
    Science. 1967 Aug 18;157(3790):804-6 PMID: 17842782
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1976-07-00
Pages
2443-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430601
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com