NDLI: Isolation and characterization of the haemin-binding proteins from Neisseria meningitidis

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Isolation and characterization of the haemin-binding proteins from Neisseria meningitidis

Content Provider	Semantic Scholar
Author	Lee, Craig
Copyright Year	2008
Abstract	Department of Microbiology and Infectious Diseases, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, Canada T2N 4N1 The mechanism of haem-iron acquisition in Neisseria meningitidis is poorly understood. Using haemin-agarose in a batch affinity chromatography method, two haemin-binding proteins of 97 and 50 kDa were isolated from total membranes derived from Neisseria meningitidis B16B6 grown under irondeficient but not under iron-replete conditions. No binding proteins were aff inity-purif ied when total membranes underwent limited proteolysis with trypsin, suggesting a haem-protein interaction. When biotinylated human haemoglobin was used as the affinity ligand, proteins of identical molecular mass were isolated. Detection of haemin-binding proteins in a whole cell binding assay demonstrated a surface-exposed location. Competitive binding studies indicated that this haem-protein interaction was specific, because only haemin or human haemoglobin, but not cytochrome clll, protoporphyrin IX, iron-loaded human lactoferrin, iron-loaded human transferrin or Fe(NO,),, could abrogate binding. The presence of similar haemin-binding proteins in a limited survey of clinical meningococcal strains indicated that the expression of the haemin-binding proteins is not serogroup-specif ic.
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Alternate Webpage(s)	http://www.microbiologyresearch.org/docserver/fulltext/micro/140/6/mic-140-6-1473.pdf?accname=guest&checksum=E40D3943B8E926A0A005FCFE8D2B28F7&expires=1541856197&id=id
Alternate Webpage(s)	https://www.microbiologyresearch.org/docserver/fulltext/micro/140/6/mic-140-6-1473.pdf?accname=guest&checksum=99A9E598A16F400813621A168A3B84E8&expires=1545948526&id=id
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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