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Bacterial Proteins and Their Proposed Interactions with Fc or Fab Fragments of Immunoglobulins | OMICS International | Abstract
ISSN: 2168-9652

Biochemistry & Physiology: Open Access
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Research Article

Bacterial Proteins and Their Proposed Interactions with Fc or Fab Fragments of Immunoglobulins

Angel Alberto Justiz Vaillant*, Sehlule Vuma and Wayne Mohammed
Pathology and Microbiology Unit, Department of Para-Clinical Sciences, The University of the West Indies, St. Augustine, Trinidad and Tobago, WI
*Corresponding Author : Angel Justiz Vaillant MD, PhD
Dept. of Para-Clinical Sciences
The University of the West Indies
St. Augustine, Trinidad & Tobago
Tel: +868-773-5914
E-mail: [email protected]; [email protected]
Received October 22, 2014; Accepted November 05, 2014; Published November 11, 2014
Citation: Vaillant AAJ, Vuma S, Mohammed W (2014) Bacterial Proteins and Their Proposed Interactions with Fc or Fab Fragments of Immunoglobulins. Biochem Physiol 3:143. doi:10.4172/2168-9652.1000143
Copyright: © 2014 Vaillant AAJ, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


The reactivity of Immunoglobulin Binding Proteins (IBP) to Fc and/or Fab fragments of immunoglobulins was summarized in this review. Staphylococcal protein A (SpA), Streptococcal protein G and Peptostreptococcal protein L (SpL) were the IBP reported. SpA reacted with IgG from skunk, coyote, raccoon, mule and donkey. SpG reacted almost with the entire panel of immunoglobulins and SpL binding was restricted to some immunoglobulins including raccoon, ostrich and duck. The various immunological techniques that have been used to test the binding capacity of IBP to Igs were double immunodiffusion, Enzyme-Linked Immunosorbent Assay (ELISA), SpA-affinity chromatography and immunoblot analysis. These protein-protein interactions are important because they can be used in the immunodiagnosis and in the purification of intact Igs or their fragments.


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