Carbohydrate Recognition Domains of Pertussis Toxin.
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概要
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Pertussis toxin (PT) is a classic "A-B" toxin produced by Bordetella pertussis; the etiologic agent of whooping cough. Like related A-B toxins, PT is composed of a single, enzymatic A subunit and a receptor-binding, B oligomer composed of five additional subunits. In most A-B toxins complex oligosaccharide sequences on glycolipids serve as host cell receptors for the B pentamer. PT is no exception but, unlike related toxins, PT also uses oligosaccharide sequences on glycoproteins as receptors in host cells. Therefore, although the enzymatic activity of the A subunit is responsible for many of PT's biological effects, the binding of its B pentamer to glycoprotein receptors can also directly alter host cell functions. Moreover, the B pentamer of PT is not composed of five identical subunits. Consequently, unlike related A-B toxins whose B pentamers are composed of identical subunits, PT is capable of recognizing several oli-gosaccharide receptor sequences. This review will summarize investigations directed at identifying host cell receptors for PT and amino acid sequences in the toxin's various carbohydrate recognition domains. Research from several laboratories indicates that PT recognizes sialated and asialo-lactosamine sequences on host cell glycoproteins and glycolipids. More recent work indicates that PT also mimics the oligosaccharide binding activities of the calcium-dependent family of eukaryotic lectins (C-lectins) which includes the selectins. Site-directed mutagenesis techniques and synthetic peptides derived from amino acid sequences in the B pentamer of PT identify regions in two of the five subunits that are probably important for coordinating carbohydrate binding.
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