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Ganglioside‐dependent cell attachment and endocytosis of murine polyomavirus‐like particles
Author(s) -
Smith Alicia E,
Lilie Hauke,
Helenius Ari
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01220-1
Subject(s) - endocytosis , ganglioside , sialic acid , sialidase , cell culture , microbiology and biotechnology , cell , biology , protease , n acetylneuraminic acid , glycolipid , biochemistry , function (biology) , chemistry , neuraminidase , enzyme , genetics
For murine polyomavirus (Py), previous studies suggest the cellular target is a terminal α2,3‐linked sialic acid. Here, we investigate the binding and uptake of mouse polyomavirus‐like particles (PyVLP) derived from bacterially expressed VP1. We find that in fibroblast 3T6 cells, binding of PyVLP was substantially reduced by sialidase treatment, but only moderately affected by protease treatment, suggesting glycolipids such as the sialic acid‐containing gangliosides mediate cell attachment. We further tested the entry requirement of PyVLP using the ganglioside‐deficient GM95 murine cell line, and find PyVLP binding and entry were reduced in these cells. Finally, we find that addition of gangliosides G M1 , G D1a , and G T1b to GM95 cells restored cellular PyVLP binding and uptake. Taken together, results indicate that gangliosides function in PyVLP cell attachment and endocytosis.