Barbara Seaton, Ph.D.

William J. Lehman, Ph.D.Professor of Physiology and Biophysics

B.S. City University of New York
Ph.D. Massachusetts Institute of Technology

Phone:(617) 638-5061
Fax: (617) 638-4273
e-mail: seatonba@bu.edu
address: see below

Research

The long-term research interests of our lab concern interactions between mammalian proteins and biomembranes or other large assemblies such as viruses. Our current focus is on the lung surfactant proteins A and D (SP-A and SP-D) and their role in innate defense against inhaled pathogens such as seasonal and pandemic strains of influenza A virus (IAV). These proteins are C-type lectins that can recognize sugars and other signature components on microbial surfaces, and can initiate events leading to pathogen neutralization. In our lab, we use x-ray crystallography, molecular modeling, and various biochemical and biophysical methods to understand the nature of these interactions at the highest resolution possible.

seaton_a

Crystal structure of the C-terminal fragment (NCRD) of unliganded SP-A NCRD trimer. Red spheres are calcium ions bound at the lectin sites.

seaton_b

Crystal structure of the human SP-D NCRD trimer with maltotriose, showing bound sugars on the top surface. Monomers shown in different colors; each binds one maltotriose and 3 calcium ions (green spheres). Arrow points to the lectin site of one of the monomers.

Selected Publications:

Seaton BA, Crouch EC, McCormack FX, Head JF, Hartshorn KL, Mendelsohn R. (2010) Structural determinants of pattern recognition by lung collectins. Innate Immun. 16: 143-150. PMID: 20423923

Crouch, E., K. Hartshorn, T. Horlacher, B. McDonald, K. Smith, T. Cafarella, B. Seaton, P. H. Seeberger, and J. Head (2009) Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343. Biochemistry 48:3335-3345. PMID:19249874

Wang H, Head J, Kosma P, Brade H, Müller-Loennies S, Sheikh S, McDonald B, Smith K, Cafarella T, Seaton B, Crou.ch E (2008) Recognition of heptoses and the inner core of bacterial lipopolysaccharides by Surfactant Protein D. Biochemistry47,710-720.

Wang L, Brauner JW, Mao G, Crouch E, Seaton B, Head J, Smith K, Flach CR, Mendelsohn R. (2008) Interaction of recombinant surfactant protein D with lipopolysaccharide: conformation and orientation of bound protein by IRRAS and simulations. Biochemistry 47, 8103-8113.

Crouch, E.C., McDonald, B., Smith, K., Mealy (Carafella), T., Seaton, B.A., Head, J.F. (2007) Critical Role of Arg/Lys343 in the Species-Dependent Recognition of Phosphatidylinositol by Pulmonary Surfactant Protein D. Biochemistry 46, 5160-5169.

Crouch, E.C., McDonald, B., Smith, K., (Mealy) Cafarella, T., Seaton, B.A., Head, J.F. (2006) Contributions of Phe335 to Carbohydrate Recognition by Human Surfactant Protein D: Stacking Interactions with Lung Collectin Ligands. J. Biol. Chem. 281, 18008-14.

Crouch, E.C., Smith, K , McDonald, B., Briner, D., Linders, B., McDonald, J., Holmskov, U., Head, J.F., Hartshorn, K. (2006) Species differences in the carbohydrate binding preferences of surfactant protein D. Am J Respir Cell Mol Biol. 35, 84-94.

Head, J.F., Mealy, T.R., McCormack, F.X., and Seaton, B.A. (2003) Crystal Structure of Trimeric Carbohydrate Recognition and Neck Domains of Surfactant Protein A. J. Biol. Chem. 278, 43254-60.

Contact Us

Department of Physiology and Biophysics
Boston University School of Medicine
72 East Concord Street
Boston MA 02118-2526

Phone:(617) 638-5061
Fax: (617) 638-4273

e-mail: seatonba@bu.edu

Directory|BUMC
September 22, 2010
Primary teaching affiliate
of BU School of Medicine