Skip to content

Research at St Andrews

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

Research output: Contribution to journalArticle

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.
Close

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

Discover related content
Find related publications, people, projects and more using interactive charts.

View graph of relations

Related by author

  1. A metalloproteomic analysis of interactions between plasma proteins and zinc: elevated fatty acid levels affect zinc distribution

    Coverdale, J. P. C., Barnett, J. P., Adamu, A. H., Griffiths, E. J., Stewart, A. J. & Blindauer, C. A., 12 Sep 2019, (Accepted/In press) In : Metallomics.

    Research output: Contribution to journalArticle

  2. Plasma non-esterified fatty acids contribute to increased coagulability in type-2 diabetes through altered plasma zinc speciation

    Sobczak, A. I. S., Katundu, K. G. H., Phoenix, F. A., Khazaipoul, S., Yu, R., Lampiao, F., Stefanowicz, F., Blindauer, C. A., Pitt, S. J., Smith, T. K., Ajjan, R. A. & Stewart, A. J., 28 Aug 2019, In : biorxiv. 38 p.

    Research output: Contribution to journalArticle

  3. Changes in plasma free fatty acids associated with type-2 diabetes

    Sobczak, A. I. S., Blindauer, C. A. & Stewart, A. J., 28 Aug 2019, In : Nutrients. 11, 9, 42 p., 2022.

    Research output: Contribution to journalReview article

  4. Sub-micromolar pulse dipolar EPR spectroscopy reveals increasing CuII-labelling of double-histidine motifs with lower temperature

    Wort, J. L., Ackermann, K., Giannoulis, A., Stewart, A. J., Norman, D. G. & Bode, B. E., 19 Aug 2019, In : Angewandte Chemie - International Edition. 58, 34, p. 11681-11685 5 p.

    Research output: Contribution to journalArticle

  5. Sub-micromolar pulse dipolar EPR spectroscopy reveals increasing CuII-labelling of double-histidine motifs with lower temperature

    Wort, J., Ackermann, K., Giannoulis, A., Stewart, A. J., Norman, D. & Bode, B. E., 19 Aug 2019, In : Angewandte Chemie. 131, 34, p. 11807-11811 6 p.

    Research output: Contribution to journalArticle

Related by journal

  1. Antimicrobial proteins: from old proteins, new tricks

    Smith, V. & Dyrynda, E., 2015, In : Molecular Immunology. 68, Issue 2, Part B, p. 383-398

    Research output: Contribution to journalArticle

  2. Determining the structure of the complex between vWF-A of factor B and CD55

    Banham, J. E., Abbott, R., Caesar, J., Roversi, P., Jeschke, G., Timmel, C. & Lea, S., Oct 2008, In : Molecular Immunology. 45, 16, p. 4122-4122 1 p.

    Research output: Contribution to journalAbstract

  3. Discovery of multiple beta-defensin like homologues in teleost fish.

    Zou, J., Mercier, C., Koussounadis, A. & Secombes, C., 2007, In : Molecular Immunology. 44, 4, p. 638-647 9 p.

    Research output: Contribution to journalArticle

ID: 20771398