Key result
A zebrafish homologue of the coxsackievirus and adenovirus receptor (zCAR) mediated infection of transfected CHO cells by both adenovirus type 5 and coxsackievirus B3.
The identification of a zebrafish CAR homologue that mediates coxsackievirus and adenovirus infection provides insights into the essential receptor contacts for viral attachment.
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zCAR mediates viral entry in heterologous cells; leaves open its physiologic role in zebrafish or human cardiac infection models.
In this study, a zebrafish homologue of the coxsackievirus and adenovirus receptor (CAR) protein was identified. Although the extracellular domain of zebrafish CAR (zCAR) is less than 50% identical to that of human CAR (hCAR), zCAR mediated infection of transfected cells by both adenovirus type 5 and coxsackievirus B3. CAR residues interacting deep within the coxsackievirus canyon are highly conserved in zCAR and hCAR, which is consistent with the idea that receptor contacts within the canyon are responsible for coxsackievirus attachment. In contrast, CAR residues contacting the south edge of the canyon are not conserved, suggesting that receptor interaction with the viral "puff region" is not essential for attachment.
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Petrella et al. (2002) studied this question. zCAR cDNA transfection vs. Mock-transfected CHO cells was evaluated on Virus attachment and infection. A zebrafish homologue of the coxsackievirus and adenovirus receptor (zCAR) mediated infection of transfected CHO cells by both adenovirus type 5 and coxsackievirus B3.
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