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Studies on the acid mucopolysaccharide coat of viruses and transformed cells
Author(s) -
Shigematsu Takeshi,
Dmochowski Leon
Publication year - 1973
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(197301)31:1<165::aid-cncr2820310123>3.0.co;2-g
Subject(s) - virus , ruthenium red , negative stain , staining , rna , hyaluronidase , microbiology and biotechnology , biology , virology , chemistry , biochemistry , enzyme , electron microscope , physics , genetics , organic chemistry , gene , optics , calcium
Ruthenium red staining method was applied to study the properties of acid mucopolysaccharides (AMPS) in cells of cultures of normal, RNA virus‐transformed, and RNA virus‐producing tumor cells. The AMPS layer of plasma membranes of virus‐transformed cells was found to be thicker than that of the plasma membrane of normal cells and more resistant to ovine hyaluronidase digestion than that of control normal cells. Hyaluronidase digestion of the AMPS layer of virus‐producing tumor cells followed by several centrifugation runs resulted in a considerable concentration of RNA virus particles. This procedure may therefore prove helpful in virus concentration studies. Ruthenium red staining revealed three distinct layers within the unit membrane of the plasma membrane of virus‐producing tumor cells as well as in the envelopes of type C and type BRNA virus particles. Study of a mouse mammary tumor (D‐W) cell line producing both type B and type C RNA virus particles after labeling by conjugated ferritin with appropriate anti‐sera and staining by ruthenium red revealed the presence of ferritin granules in the AMPS layer of these particles. As demonstrated by ruthenium red staining, the functional and immunologic properties of the AMPS layer on virus particles are as follows: it plays at least a part in the adherance of RNA virus particles to the plasma membrane of cells; acts as a protective layer of virus particles against enzymatic damage, and it is a site of viral antigen‐antibody reactions. This study has also demonstrated similarities in the ultrastructure of plasma membrane of RNA virus‐transformed and virus‐producing tumor cells and of the envelope of RNA type B and type C virus particles.