Identification and characterization of functional subunits of Clostridium botulinum type A progenitor toxin involved in binding to intestinal microvilli and erythrocytes

FEBS Letters

Inoue, Kaoru²  Oguma, Keiji²  Kozaki, Shunji³  Fujinaga, Yukako²  Nomura, Takako⁴  Popoff, Michel R.¹  Marvaud, Jean C.¹  Sasaki, Junzo⁴ 

[1] Unite des Toxines Microbiennes, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France;Department of Bacteriology, Okayama University Medical School, 2-5-1 Shikata-cho, Okayama 700-8558, Japan;Department of Veterinary Science, College of Agriculture, University of Osake Prefecture, 1-1 Gakuen-cho, Sakai, Osaka 599-8231, Japan;Department of Anatomy, Okayama University Medical School, 2-5-1 Shikata-cho, Okayama 700-8558, Japan

关键词: Toxin binding;    Hemagglutinin;    Microvillus;    Clostridium botulinum;   

DOI  :  10.1016/S0014-5793(00)01147-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Clostridium botulinum type A hemagglutinin-positive progenitor toxin consists of three distinct components: neurotoxin (NTX), hemagglutinin (HA), and non-toxic non-HA (NTNH). The HA consists of four subcomponents designated HA1, 2, 3a and 3b. By employing purified toxin and GST-fusion proteins of each HA subcomponent, we found that the HA-positive progenitor toxin, GST-HA1 and GST-HA3b bind to human erythrocytes and microvilli of guinea pig upper small intestinal sections. The HA-positive progenitor toxin and GST-HA1 bind via galactose moieties, GST-HA3b binds via sialic acid moieties. GST-2 and GST-3a showed no detectable binding.

【 授权许可】

Unknown