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Current Pediatric Reviews
ISSN (Print): 1573-3963
ISSN (Online): 1573-7829
VOLUME: 9
ISSUE: 4
DOI: 10.2174/157339630904131223105730      Price:  $58









Mycoplasma pneumoniae Attachment Proteins and Toxins as Mediators in Disease Production

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Author(s): Mitchell F. Balish
Pages 296-303 (8)
Abstract:
In order to cause disease, Mycoplasma pneumoniae must adhere to host cells and produce cytotoxic molecules. Despite its small genome, M. pneumoniae achieves cytadherence through the synthesis of a complex cellular structure, the terminal organelle or attachment organelle, which initiates binding to host cells through carbohydrate moieties associated with protein and lipid molecules on their surfaces. The construction of this organelle is remarkable, making use of proteins that are generally dissimilar in composition to those found in organisms other than the closest relatives of M. pneumoniae. The attachment organelle also plays an essential role in the crucial but poorly understood process of gliding motility. Cytadherence is also carried out by other proteins involved in binding to ligands found on host cell surfaces. Having accomplished cytadherence, M. pneumoniae damages host cells though various means. One is production of hydrogen peroxide, which occurs via metabolism of glycerol. Another is the production of CARDS toxin, an ADPribosyltransferase that induces vacuolation and, when administered on its own, mimics many of the clinical symptoms of M. pneumoniae-associated disease. A nuclease has been implicated in promoting apoptosis of host cells. Finally, certain M. pneumoniae lipoproteins elicit host immunologic responses that contribute significantly to cytokine production and concomitant inflammation. These various virulence factors make M. pneumoniae difficult to clear, resulting in not just acute but also chronic disease.
Keywords:
Adhesin, ADP-ribosylating toxin, attachment organelle, hydrogen peroxide, lipoprotein, Mycoplasma pneumoniae.
Affiliation:
Department of Microbiology, Miami University, Oxford, OH 45056, USA.