MHC class I molecules are enriched in caveolae but do not enter with simian virus 40.

Anderson, Howard A.; Chen, Yuzhi; Norkin, Leonard C.

doi:10.1099/0022-1317-79-6-1469

Cited by 67 publications

(49 citation statements)

References 54 publications

(59 reference statements)

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“…Whether the coupling involves the lipids alone or also proteins on the inside surface of the PM remains to be determined. A fraction of virions enters caveolar invaginations that are rich in signaling molecules at the plasma membrane (Anderson et al 1996(Anderson et al , 1998Stang et al 1997), and the addition of SV40 particles activates caveolar trafficking (Tagawa et al 2005). However, while shRNA against Caveolin-1 reduces infection significantly in HeLa cells , Caveolin-1 deficient cells are readily infected and internalize SV40 at an even faster rate than wt cells (Damm et al 2005).…”

Section: Lipid-mediated Endocytosismentioning

confidence: 99%

Lipid-Mediated Endocytosis

Ewers¹,

Helenius²

2011

Cold Spring Harbor Perspectives in Biology

157

133

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Section: Lipid-mediated Endocytosismentioning

confidence: 99%

Lipid-Mediated Endocytosis

Ewers¹,

Helenius²

2011

Cold Spring Harbor Perspectives in Biology

157

133

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“…Although SV40 can attach to major histocompatibility complex class I molecules (8,9), these are not endocytosed with the virus (10). By contrast, engagement of gangliosides leads to virion uptake via cholesterol-dependent endocytosis and transport to the endoplasmic reticulum (ER), an essential step on the infectious route (11)(12)(13)(14).…”

mentioning

confidence: 99%

Structural basis of GM1 ganglioside recognition by simian virus 40

Neu

Woellner

Gauglitz

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

168

229

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Simian virus 40 (SV40) has been a paradigm for understanding attachment and entry of nonenveloped viruses, viral DNA replication, and virus assembly, as well as for endocytosis pathways associated with caveolin and cholesterol. We find by glycan array screening that SV40 recognizes its ganglioside receptor GM1 with a quite narrow specificity, but isothermal titration calorimetry shows that individual binding sites have a relatively low affinity, with a millimolar dissociation constant. The high-resolution crystal structure of recombinantly produced SV40 capsid protein, VP1, in complex with the carbohydrate portion of GM1, reveals that the receptor is bound in a shallow solvent-exposed groove at the outer surface of the capsid. Through a complex network of interactions, VP1 recognizes a conformation of GM1 that is the dominant one in solution. Analysis of contacts provides a structural basis for the observed specificity and suggests binding mechanisms for additional physiologically relevant GM1 variants. Comparison with murine Polyomavirus (Polyoma) receptor complexes reveals that SV40 uses a different mechanism of sialic acid binding, which has implications for receptor binding of human polyomaviruses. The SV40 -GM1 complex reveals a parallel to cholera toxin, which uses a similar cell entry pathway and binds GM1 in the same conformation.crystal structure ͉ glycan array ͉ polyomaviruses ͉ viral attachment ͉ protein-carbohydrate complex

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“…We also cannot exclude the possibility that the presence of MHC class I molecules at the plasma membrane could recruit the negative PKB/Akt regulator, i.e., phosphatase and tensin homologue deleted on chromosome 10 (PTEN), to this cellular location and preclude the basal high activity of PKB/Akt. Both MHC class I glycoproteins and PTEN molecules are associated with detergent-insoluble microdomains (lipid rafts) of the plasma membrane (45,46) and the precise composition of rafts has been shown to be determinative for PKB/Akt activity (47,48). Moreover, it has been shown that even in PTEN-deficient tumor cells the activity of PKB/Akt is still subject to down-regulation via alterations in cell membrane rafts (49).…”

Section: Discussionmentioning

confidence: 99%

Alterations in the Expression of MHC Class I Glycoproteins by B16BL6 Melanoma Cells Modulate Insulin Receptor-Regulated Signal Transduction and Augments Resistance to Apoptosis

Assa-Kunik

Fishman

Kellman-Pressman

et al. 2003

The Journal of Immunology

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In a variety of malignancies, the immune-escape phenotype is associated, in part, with the inability of tumor cells to properly present their Ags to CTLs due to a deranged expression of MHC class I glycoproteins. However, these molecules were found to possess broader nonimmune functions, including participation in signal transduction and regulation of proliferation, differentiation, and sensitivity to apoptosis-inducing factors; processes, which are characteristically impaired during malignant transformation. We investigated whether the deranged expression of MHC class I expression by tumor cells could affect proper receptor-mediated signal transduction and accentuate their malignant phenotype. The malignant and H-2K murine MHC class I-deficient B16BL6 melanoma cells were characterized by an attenuated capacity to bind insulin due to the retention of corresponding receptor in intracellular stores. The restoration of H-2K expression in these cells, which abrogated their capacity to form tumors in mice, enhanced membrane translocation of the receptor, presumably, by modulating its glycosylation. The addition of insulin to H-2K-expressing melanoma cells cultured in serum-free conditions precluded apoptotic death by up-regulating the activity of protein kinase B (PKB)/Akt. In contrast, the deficiency for H-2K characteristic to the malignant clones was associated with a constitutive high activity of PKB/Akt, which rendered them resistant to apoptosis, induced by deprivation of serum-derived growth factors. The possibility to correct the regulation of PKB/Akt activity by restoration of H-2K expression in B16BL6 melanoma cells may be considered as an attractive approach for cancer therapy, since an aberrant activation of this enzyme is characteristic to resistant malignancies.

show abstract

MHC class I molecules are enriched in caveolae but do not enter with simian virus 40.

Cited by 67 publications

References 54 publications

Lipid-Mediated Endocytosis

Lipid-Mediated Endocytosis

Structural basis of GM1 ganglioside recognition by simian virus 40

Alterations in the Expression of MHC Class I Glycoproteins by B16BL6 Melanoma Cells Modulate Insulin Receptor-Regulated Signal Transduction and Augments Resistance to Apoptosis

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