Crystallization and X-ray diffraction analysis of a novel surface-adhesin protein: protein E from Haemophilus influenzae.
Författare
Summary, in English
Protein E (PE) is a ubiquitous multifunctional surface protein of Haemophilus spp. and other bacterial pathogens of the Pasteurellaceae family. H. influenzae utilizes PE for attachment to respiratory epithelial cells. In addition, PE interacts directly with plasminogen and the extracellular matrix (ECM) components vitronectin and laminin. Vitronectin is a complement regulator that inhibits the formation of the membrane-attack complex (MAC). PE-mediated vitronectin recruitment at the H. influenzae surface thus inhibits MAC and protects against serum bactericidal activity. Laminin is an abundant ECM protein and is present in the basement membrane that helps in adherence of H. influenzae during colonization. Here, the expression, purification and crystallization of and the collection of high-resolution data for this important H. influenzae adhesin are reported. To solve the phase problem for PE, Met residues were introduced and an SeMet variant was expressed and crystallized. Both native and SeMet-containing PE gave plate-like crystals in space group P2(1), with unit-cell parameters a = 44, b = 57, c = 61 Å, β = 96°. Diffraction data collected from native and SeMet-derivative crystals extended to resolutions of 1.8 and 2.6 Å, respectively.
Avdelning/ar
- Klinisk mikrobiologi, Malmö
- Geriatric Medicine
- Geriatrik
Publiceringsår
2012
Språk
Engelska
Sidor
222-226
Publikation/Tidskrift/Serie
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Volym
68
Issue
Pt 2
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Wiley-Blackwell
Ämne
- Microbiology in the medical area
- Gerontology, specializing in Medical and Health Sciences
Status
Published
Forskningsgrupp
- Clinical Microbiology, Malmö
- Geriatric Medicine
- Geriatrics
ISBN/ISSN/Övrigt
- ISSN: 2053-230X