Induction of CTLin vivo by major histocompatibility complex class I-peptide complexes covalently associated on the cell surface

1995 ◽  
Vol 25 (6) ◽  
pp. 1535-1540 ◽  
Author(s):  
Fabienne Anjuère ◽  
Clotilde Horvath ◽  
Jean-Charles Cerottini ◽  
Immanuel F. Luescher
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Peptide Complexes

Major histocompatibility complex class I-binding peptides are recycled to the cell surface after internalization

1993 ◽  
Vol 23 (12) ◽  
pp. 3224-3229 ◽  
Author(s):  
Ussama M. Abdel Motal ◽  
Xianzheng Zhou ◽  
Annalena Joki ◽  
Abdur Rehman Siddiqi ◽  
B. R. Srinivasa ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Binding Peptides

scholarly journals GRP78, a Coreceptor for Coxsackievirus A9, Interacts with Major Histocompatibility Complex Class I Molecules Which Mediate Virus Internalization

2002 ◽  
Vol 76 (2) ◽  
pp. 633-643 ◽  
Author(s):  
Kathy Triantafilou ◽  
Didier Fradelizi ◽  
Keith Wilson ◽  
Martha Triantafilou
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Class I Mhc ◽  
Mhc I ◽  
Histocompatibility Complex ◽  
Coxsackievirus A9

ABSTRACT It is becoming apparent that over the years cell infection by virus seems to have evolved into a multistep process in which many viruses employ distinct cell surface molecules for their attachment and cell entry. In this study the attachment and entry pathway of coxsackievirus A9 (CAV-9), a member of the Picornaviridae family, was investigated. It has been known that, although integrin αvβ3 is utilized as a receptor, its presence alone is insufficient for CAV-9 infection and that CAV-9 also requires a 70-kDa major histocompatibility complex class I (MHC-I)-associated protein (MAP-70) as a coreceptor molecule. We document by protein isolation and peptide sequencing that the 70-kDa protein is GRP78, a member of the heat shock protein 70 family of stress proteins. Furthermore we show by using fluorescence resonance energy transfer (FRET) that GRP78 is also expressed on the cell surface and associates with MHC-I molecules. In addition CAV-9 infection of permissive cells requires GRP78 and also MHC-I molecules, which are essential for virus internalization. The identification of GRP78 as a coreceptor for CAV-9 and the revelation of GRP78 and MHC-I associations have provided new insights into the life cycle of CAV-9, which utilizes integrin αvβ3 and GRP78 as receptor molecules whereas MHC-I molecules serve as the internalization pathway of this virus to mammalian cells.

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