Isolation of a putative laminin binding protein from Streptococcus anginosus. Academic Article

abstract

• Viridans streptococci, including Streptococcus anginosus, are a common cause of infective endocarditis in humans. Adherence mechanisms involved in colonization of non-diseased native valves (present in 40% of native valve endocarditis) are unknown. We have previously shown that an endocarditis isolate of S. anginosus adheres to exposed basement membrane of human and porcine valve tissue in a laminin dependent manner. We now describe the partial purification of an 80 kDa putative laminin binding protein (PLBP) by biochemical methods. Amino acid sequence of PLBP peptides is similar to substrate binding proteins of ABC transporters in other Gram-positive cocci.

authors

• Hook, Magnus

published proceedings

• Microb Pathog

author list (cited authors)

• Allen, B. L., & Hk, M.

citation count

• 14

complete list of authors

• Allen, Bradley L||Höök, Magnus

publication date

• January 2002

publisher

• Elsevier  Publisher

published in

• Microbial Pathogenesis  Journal

keywords

• Amino Acid Sequence
• Antibodies
• Bacterial Adhesion
• Bacterial Proteins
• Electrophoresis, Polyacrylamide Gel
• Endocarditis, Bacterial
• Humans
• Molecular Sequence Data
• Molecular Weight
• Receptors, Laminin
• Sequence Analysis, Protein
• Sequence Homology, Amino Acid
• Streptococcus Anginosus

Digital Object Identifier (DOI)

• 10.1006/mpat.2002.0510

start page

• 23

end page

• 31

volume

• 33

issue

• 1

URL

• http://dx.doi.org/10.1006/mpat.2002.0510