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Structural and immunologic characterization of bovine, horse, and rabbit serum albumins

Research output: Contribution to journalArticlepeer-review

Author(s)

Karolina A. Majorek, Przemyslaw J. Porebski, Arjun Dayal, Matthew D. Zimmerman, Kamila Jablonska, Alan J. Stewart, Maksymilian Chruszcz, Wladek Minor

School/Research organisations

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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Details

Original languageEnglish
Pages (from-to)174-182
Number of pages9
JournalMolecular Immunology
Volume52
Issue number3-4
Early online date6 Jun 2012
DOIs
Publication statusPublished - 1 Oct 2012

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