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Crystallization and X-ray diffraction analysis of a novel surface-adhesin protein: protein E from Haemophilus influenzae.

In English

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

Publiceringsår

2012

Språk

Engelska

Sidor

222-226

Publikation/Tidskrift/Serie

Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Volym

68

Issue

Pt 2

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