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Title of Journal: Glycoconj J

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Abbravation: Glycoconjugate Journal

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Springer US

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10.1016/0307-904x(81)90043-3

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1573-4986

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Exquisite binding specificity of Emphasis Type="I

Authors: Vishwanath B Chachadi Shashikala R Inamdar LuGang Yu Jonathan M Rhodes Bale M Swamy
Publish Date: 2011/02/24
Volume: 28, Issue: 1, Pages: 49-56
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Abstract

Sclerotium rolfsii lectin SRL a secretory protein from the soil borne phytopathogenic fungus Sclerotium rolfsii has shown in our previous studies to bind strongly to the oncofetal ThomsonFriedenreich carbohydrate Galβ13GalNAcser/thr T or TF antigen TF antigen is widely expressed in many types of human cancers and the strong binding of SRL toward such a cancerassociated carbohydrate structure led us to characterize the carbohydrate binding specificity of SRL Glycan array analysis which included 285 glycans shows exclusive binding of SRL to the Olinked mucin type but not Nlinked glycans and amongst the mucin type Oglycans lectin recognizes only mucin core 1 core 2 and weakly core 8 but not to other mucin core structures It binds with high specificity to “αanomers” but not the “βanomers” of the TF structure The axial C4OH group of GalNAc and C2OH group of Gal is both essential for SRL interaction with TF disaccharide and substitution on C3 of galactose by sulfate or sialic acid or Nacetylglucosamine significantly enhances the avidity of the lectin SRL differs in its binding to TF structures compared to other known TFbinding lectins such as the Arachis hypogea peanut agglutinin Agaricus bisporus mushroom lectin Jackfruit Artocarpus integrifolia jacalin and Amaranthus caudatus Amaranthin lectin Thus SRL has unique carbohydratebinding specificity toward TFrelated Olinked carbohydrate structures Such a binding specificity will make this lectin a very useful tool in future structural as well as functional analysis of the cellular glycans in cancer studies


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