Citation

Krane S, Itagaki Y, Nakanishi K, Weldon PJ. Naturwissenschaften 2003; 90(2): 60-62.

Affiliation

Department of Chemistry, Columbia University, New York, NY 10027, USA.

Copyright

(Copyright © 2003, Holtzbrinck Springer Nature Publishing Group)

DOI

10.1007/s00114-002-0394-z

PMID

12590298

Abstract

Bites inflicted on humans by the slow loris (Nycticebus coucang), a prosimian from Indonesia, are painful and elicit anaphylaxis. Toxins from N. coucang are thought to originate in the brachial organ, a naked, gland-laden area of skin situated on the flexor surface of the arm that is licked during grooming. We isolated a major component of the brachial organ secretions from N. coucang, an approximately 18 kDa protein composed of two 70-90 amino-acid chains linked by one or more disulfide bonds. The N-termini of these peptide chains exhibit nearly 70% sequence similarity (37% identity, chain 1; 54% identity, chain 2) with the two chains of Fel d 1, the major allergen from the domestic cat (Felis catus). The extensive sequence similarity between the brachial organ component of N. coucang and the cat allergen suggests that they exhibit immunogenic cross-reactivity. This work clarifies the chemical nature of the brachial organ exudate and suggests a possible mode of action underlying the noxious effects of slow loris bites.

Language: en