Breakdown of albumin and haemalbumin by the cysteine protease interpain A, an albuminase of Prevotella intermedia

BMC Microbiology

John W. Smalley¹  Jan Potempa³  Surya P. Manandhar⁴  Dominic P. Byrne² 

[1] The University of Liverpool, School of Dentistry, Daulby Street, Liverpool L69 3GN, UK;Department of Biochemistry, Institute of Integrative Biology, The University of Liverpool, Crown Street, Liverpool L69 7ZB, UK;Department of Oral Immunology and Infectious Diseases, University of Louisville School of Dentistry, 501 S. Preston St., Louisville 40202, KY, USA;Department of Biological Sciences, California State University Long Beach, 1250 Bellflower Blvd., Long Beach 90840, California, USA

关键词: Prevotella intermedia;    Interpain A;    Haem;    Periodontal disease;    Protease;    Albumin;   

Others  :  1227549
DOI  :  10.1186/s12866-015-0516-3

 received in 2015-05-07, accepted in 2015-09-09,  发布年份 2015

【 摘 要 】

Background

Prevotella intermedia is a Gram-negative black-pigmenting oral anaerobe associated with periodontitis in humans, and has a haem requirement for growth, survival and virulence. It produces an iron porphyrin-containing pigment comprising monomeric iron (III) protoporphyrin IX (Fe(III)PPIX.OH; haematin). The bacterium expresses a 90-kDa cysteine protease termed interpain A (InpA) which both oxidizes and subsequently degrades haemoglobin, releasing haem. However, it is not known whether the enzyme may play a role in degrading other haem-carrying plasma proteins present in the gingival sulcus or periodontal pocket from which to derive haem. This study evaluated the ability of InpA to degrade apo- and haem-complexed albumin.

Results

Albumin breakdown was examined over a range of pH and in the presence of reducing agent; conditions which prevail in sub- and supra-gingival plaque. InpA digested haemalbumin more efficiently than apoalbumin, especially under reducing conditions at pH 7.5. Under these conditions InpA was able to substantially degrade the albumin component of whole human plasma.

Conclusions

The data point to InpA as an efficient “albuminase” with the ability to degrade the minor fraction of haem-bound albumin in plasma. InpA may thus contribute significantly to haem acquisition by P. intermedia under conditions of low redox potential and higher pH in the inflamed gingival crevice and diseased periodontal pocket where haem availability is tightly controlled by the host.

【 授权许可】

   
2015 Byrne et al.

【 图 表 】

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