Molecular immunology2012; 52(3-4); 174-182; doi: 10.1016/j.molimm.2012.05.011

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

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.
Publication Date: 2012-06-06 PubMed ID: 22677715PubMed Central: PMC3401331DOI: 10.1016/j.molimm.2012.05.011Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • N.I.H.
  • Extramural
  • Research Support
  • Non-U.S. Gov't

Summary

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This research study investigates the structural and immunological characteristics of serum albumins (SA) – a type of protein commonly found in the blood plasma of mammals – from cattle, horses, and rabbits. The researchers not only examined the physical structure of these proteins, but also looked at how they interact with the immune system and their potential for causing allergic reactions.

Explanation of Serum Albumins

  • Serum albumins are multifunctional proteins that play an important role in transporting a variety of substances throughout the body. These substances can include metabolites, drugs, nutrients, metals, and other molecules.
  • Due to the ability of these proteins to bind to a wide range of substances, they have various applications in the medical, pharmaceutical, and biochemical fields.
  • However, albumins have been known to cause allergic reactions in some individuals, due to their similar structure and sequence in different organisms – a phenomenon known as “cross-reactivity”.

Research Methodology

  • The research team presented crystal structures of SAs from cattle (bovine serum albumin or BSA), horse (equine serum albumin or ESA), and rabbit (rabbit serum albumin or RSA).
  • They analyzed the conservation or divergence of their structural and sequential information, in relation to their potential allergenicity and cross-reactivity.

Research Findings

  • In their analysis, the researchers observed variations in the structures and sequences of the albumins from the three different species.
  • They discovered a previously unknown ligand binding site within the structure of the rabbit’s serum albumin and also identified the presence of calcium binding sites within the bovine serum albumin. The latter is noteworthy as it is the first instance of a serum albumin structure being found to contain metal ions.

Significance of the Study

  • The findings of this study provide further insight into the structural and immunological characteristics of serum albumins from different species. This could have implications for the design of new drugs and the development of therapeutic strategies.
  • The identification of a new ligand binding site and calcium binding sites in serum albumins increases our understanding of these proteins and could pave the way for future research in the field.

Cite This Article

APA
Majorek KA, Porebski PJ, Dayal A, Zimmerman MD, Jablonska K, Stewart AJ, Chruszcz M, Minor W. (2012). Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. Mol Immunol, 52(3-4), 174-182. https://doi.org/10.1016/j.molimm.2012.05.011

Publication

ISSN: 1872-9142
NlmUniqueID: 7905289
Country: England
Language: English
Volume: 52
Issue: 3-4
Pages: 174-182

Researcher Affiliations

Majorek, Karolina A
  • Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.
Porebski, Przemyslaw J
    Dayal, Arjun
      Zimmerman, Matthew D
        Jablonska, Kamila
          Stewart, Alan J
            Chruszcz, Maksymilian
              Minor, Wladek

                MeSH Terms

                • Amino Acid Sequence
                • Animals
                • Binding Sites
                • Calcium / metabolism
                • Calcium-Binding Proteins / metabolism
                • Cattle / blood
                • Crystallization
                • Horses / blood
                • Hypersensitivity / immunology
                • Models, Molecular
                • Molecular Sequence Data
                • Protein Binding
                • Protein Structure, Secondary
                • Rabbits / blood
                • Sequence Alignment
                • Sequence Analysis, Protein
                • Serum Albumin / chemistry
                • Serum Albumin / immunology
                • Species Specificity

                Grant Funding

                • U54 GM094662 / NIGMS NIH HHS
                • GM094662 / NIGMS NIH HHS

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