TY - JOUR
T1 - Structural and immunologic characterization of bovine, horse, and rabbit serum albumins
AU - Majorek, Karolina A.
AU - Porebski, Przemyslaw J.
AU - Dayal, Arjun
AU - Zimmerman, Matthew D.
AU - Jablonska, Kamila
AU - Stewart, Alan J.
AU - Chruszcz, Maksymilian
AU - Minor, Wladek
N1 - Funding Information:
The authors would like to thank Alexander Wlodawer and Heimo Breiteneder for critical reading of the manuscript. We would like to thank Steve Almo and members of New York Structural Genomics Research Consortium for their contribution to this work. The work described here was supported by the NIH Protein Structure Initiative grant GM094662 . The structural results shown in this report are derived from work performed at the Argonne National Laboratory, at the Structural Biology Center and Life Sciences Collaborative Access Team of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor for the support of this research program grant ( 085P1000817 ).
PY - 2012/10
Y1 - 2012/10
N2 - 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.
AB - 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.
KW - Allergen
KW - Bovine serum albumin (BSA)
KW - Calcium binding
KW - Cross-reactivity
KW - Equine serum albumin (ESA)
KW - Rabbit serum albumin (RSA)
KW - Serum albumin (SA)
UR - http://www.scopus.com/inward/record.url?scp=84861792561&partnerID=8YFLogxK
U2 - 10.1016/j.molimm.2012.05.011
DO - 10.1016/j.molimm.2012.05.011
M3 - Article
C2 - 22677715
AN - SCOPUS:84861792561
SN - 0161-5890
VL - 52
SP - 174
EP - 182
JO - Molecular Immunology
JF - Molecular Immunology
IS - 3-4
ER -