A zebrafish coxsackievirus and adenovirus receptor homologue interacts with coxsackie B virus and adenovirus.
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.
Petrella
JenniElizabeth
J
Division of Immunologic and Infectious Diseases, The Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, USA.
Cohen
Christopher J
CJ
Gaetz
Jedidiah
J
Bergelson
Jeffrey M
JM
D000260:Adenoviruses, Human / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D016466:CHO Cells; D017124:Conserved Sequence; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D006224:Cricetinae; D018076:DNA, Complementary; D029822:Enterovirus B, Human / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism*; D015027:Zebrafish
C568771:CLMP protein, human; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D018076:DNA, Complementary; D011991:Receptors, Virus