, Volume 90, Issue 2, pp 60–62 | Cite as

"Venom" of the slow loris: sequence similarity of prosimian skin gland protein and Fel d 1 cat allergen

  • Sonja Krane
  • Yasuhiro Itagaki
  • Koji NakanishiEmail author
  • Paul J. Weldon
Short Communication


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.


High Performance Liquid Chromatography Felis Atmospheric Pressure Chemical Ionization Loris Major Allergen 
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C. Lehn, M. Linn, and C. McCann (Wildlife Conservation Society, Bronx, New York) permitted access to the slow loris or assisted in sample collection. B. Lester (Houston Zoo, Texas) provided several important references.


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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  • Sonja Krane
    • 1
  • Yasuhiro Itagaki
    • 1
  • Koji Nakanishi
    • 1
    Email author
  • Paul J. Weldon
    • 2
  1. 1.Department of ChemistryColumbia UniversityNew YorkUSA
  2. 2.Conservation and Research CenterSmithsonian InstitutionFront RoyalUSA

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