Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim Biophys Acta 2011 Jan;1808(1):482-9
Date
10/05/2010Pubmed ID
20883662Pubmed Central ID
PMC2997907DOI
10.1016/j.bbamem.2010.09.017Scopus ID
2-s2.0-78649779510 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
Ail is an outer membrane protein and virulence factor of Yersinia pestis, an extremely pathogenic, category A biothreat agent, responsible for precipitating massive human plague pandemics throughout history. Due to its key role in bacterial adhesion to host cells and bacterial resistance to host defense, Ail is a key target for anti-plague therapy. However, little information is available about the molecular aspects of its function and interactions with the human host, and the structure of Ail is not known. Here we describe the recombinant expression, purification, refolding, and sample preparation of Ail for solution and solid-state NMR structural studies in lipid micelles and lipid bilayers. The initial NMR and CD spectra show that Ail adopts a well-defined transmembrane β-sheet conformation in lipids.
Author List
Plesniak LA, Mahalakshmi R, Rypien C, Yang Y, Racic J, Marassi FMAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceBacterial Adhesion
Bacterial Outer Membrane Proteins
Circular Dichroism
Gene Expression Regulation, Bacterial
Hydrogen-Ion Concentration
Lipids
Magnetic Resonance Spectroscopy
Molecular Conformation
Molecular Sequence Data
Protein Folding
Protein Structure, Secondary
Sequence Homology, Amino Acid
Virulence Factors
Yersinia pestis
