Coxsackie B virus and its interaction with permissive host cells.
BACKGROUND
Observations in humans and the results of experiments on laboratory animals have provided evidence that coxsackieviruses of group B (CVB) are major etiologic agents of acute and chronic enterovirus myocarditis and various other virus-induced diseases.


OBJECTIVE
This minireview briefly summarizes the investigations to elucidate various molecular mechanisms for the induction and maintenance of persistent CVB infections. With regard to the recent findings that CVB may use several different receptor proteins, this article focuses on virus-host cell interactions and the potential impact of these interactions for enteroviral replication.


METHODS
The interaction of CVB with specific cell surface proteins was analyzed in cultured cell lines and murine tissues at the level of virus attachment and virus internalization. As example for the interaction of CVB with intracellular proteins, the state of p21rasGTPase-activating protein (RasGAP) was investigated in mock-infected and CVB3-infected HeLa cells.


CONCLUSIONS
The experiments to elucidate the virus receptor interactions revealed the necessity to differentiate between CVB attachment proteins and proteins involved in virus internalization. Since more than one protein may be required to initiate the uptake of CVB into permissive host cells, a model of the putative interaction of these proteins within a multimeric receptor complex is proposed. It is further tempting to speculate that the presence of multiple attachment proteins may influence the tissue tropism of CVB as well as pathogenicity.
Selinka
H C
HC
Department of Molecular Pathology, University of Tübingen, Germany. hans-christoph.selinka@med.uni-tuebingen.de
Huber
M
M
Pasch
A
A
Klingel
K
K
Aepinus
C
C
Kandolf
R
R
D000818:Animals; D003384:Coxsackievirus Infections / Q000503:physiopathology; D029822:Enterovirus B, Human / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D007424:Intracellular Fluid; D008565:Membrane Proteins / Q000378:metabolism; D017735:Virus Latency
D008565:Membrane Proteins