Structural and Immunologic Characterization of Bovine, Horse, and Rabbit Serum Albumins

Overview

Journal Mol Immunol

Specialties Allergy & Immunology
Molecular Biology

Date 2012 Jun 9

PMID 22677715

Citations 198

Authors

Karolina A Majorek

Przemyslaw J Porebski

Arjun Dayal

Matthew D Zimmerman

Kamila Jablonska

Alan J Stewart

Maksymilian Chruszcz

Wladek Minor

Affiliations

Soon will be listed here.

Abstract

Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to its ligand binding properties, albumins have wide clinical, pharmaceutical, and biochemical applications. Albumins are also allergenic, and exhibit a high degree of cross-reactivity due to significant sequence and structure similarity of SAs from different organisms. Here we present crystal structures of albumins from cattle (BSA), horse (ESA) and rabbit (RSA) sera. The structural data are correlated with the results of immunological studies of SAs. We also analyze the conservation or divergence of structures and sequences of SAs in the context of their potential allergenicity and cross-reactivity. In addition, we identified a previously uncharacterized ligand binding site in the structure of RSA, and calcium binding sites in the structure of BSA, which is the first serum albumin structure to contain metal ions.

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