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R-Type Lectin Families

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Book cover Animal Lectins: Form, Function and Clinical Applications

Abstract

The R-type lectins are members of a superfamily of proteins, all of which contain a carbohydrate-recognition domain (CRD) that is structurally similar to the CRD in Ricin. The R-type domain is an ancient type of protein fold that is found in many glycosyltransferases as well as in bacterial and fungal hydrolases. Interestingly, the R-type CRD is the only one conserved between animal and bacterial lectins (Sharon and Lis 2004). Ricin was the first lectin discovered and it is the prototypical lectin in this category. Two different lectins have been purified from R. communis seeds, and in the original nomenclature they were termed RCA-I and RCA-II. RCA-I is an agglutinin but a very weak toxin. RCA-II is commonly called ricin, and it is both an agglutinin and a very potent toxin. The designation RCA-II has now been dropped, but the original name for the agglutinin RCA-I has been retained. The molecular mass of RCA-I is approximately 120 kDa and that of ricin is approximately 60-kDa. Ricin is a type II ribosome-inactivating protein (RIP-II). Although one might predict that RCA-I also would be highly toxic, it has weak activity compared to ricin because it lacks a separate A chain (Fig. 14.1).

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  1. Vaccine Production Division, Panacea Biotec, Lalru (Mohali), Punjab, India

    Rajesh K. Gupta (General Manager)

  2. Department of Biophysics, Punjab University, Chandigarh, India

    G. S. Gupta (Former Professor and Chairman)

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Gupta, R.K., Gupta, G.S. (2012). R-Type Lectin Families. In: Animal Lectins: Form, Function and Clinical Applications. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1065-2_14

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