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Critical Reviews in Oral Biology & Medicine
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ORAL MICROBIAL HEAT-SHOCK PROTEINS AND THEIR POTENTIAL CONTRIBUTIONS TO INFECTIONS

Florence Goulhen1, Daniel Grenier2,* and Denis Mayrand1

1 Groupe de Recherche en Écologie Buccale, Faculté des Sciences et de Génie and
2 Faculté de Médecine Dentaire, Université Laval, Cité universitaire, Quebec City, Quebec, Canada, G1K 7P4;


Figure 1
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  		Figure 1. Immunolocalization by transmission electron microscopy of GroEL in ultrathin sections of A. actinomycetemcomitans ATCC 29522. Unstressed cells (Panel A) and heat-stressed cells (30 min at 43°C) (Panel B) were labeled with use of a specific antibody raised against the purified A. actinomycetemcomitans ATCC 29522 GroEL. More gold particles are observed both inside and outside stressed bacteria compared with unstressed bacteria.

 

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  		Figure 2. Transmission electron micrograph of the purified native A. actinomycetemcomitans ATCC 29522 GroEL stained with uranyl acetate. The heptameric ring can be seen in the enlargement. Bar = 20 nm.

 

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  		Figure 3. Phylograms of HSP10 (Panel A), HSP60 (Panel B), HSP70 (Panel C), and HSP90 (Panel D) from various micro-organisms, including oral bacteria. The bar represents the number of mutations per site.

 

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  		Figure 4. Immunoreactivity of human fibronectin with antibodies directed against bacterial GroEL and human HSP60. (Lane 1) A. actinomycetemcomitans GroEL (0.02 µg). (Lane 2) Human plasma fibronectin (1.67 µg). (Lane 3) Fibroblast fibronectin (0.02 µg). (Lane 4) E. coli GroEL (0.01 µg). (Lane 5) Human plasma fibronectin (1.67 µg). (Lane 6) Human HSP60 (0.01 µg). (Lane 7) Human plasma fibronectin (1.67 µg). Lanes 1–3 were probed with pAb-AaGroEL. Lanes 4 and 5 were probed with pAb-EcGroEL. Lanes 6 and 7 were probed with mAb-HuHSP60.

 

Critical Reviews in Oral Biology & Medicine, Vol. 14, No. 6, 399-412 (2003)
DOI: 10.1177/154411130301400603
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