Adsorption of Mycoplasma pneumoniae to neuraminic acid receptors of various cells and possible role in virulence.
Monkey, rat, and chicken tracheal epithelial cells, as well as monkey, rat, guinea pig, and chicken erythrocytes, adsorbed firmly to colonies of Mycoplasma pneumoniae and M. gallisepticum. Colonies of M. pulmonis also adsorbed erythrocytes but with less avidity than M. pneumoniae or M. gallisepticum; unlike the latter organisms, M. pulmonis did not adsorb tracheal epithelial cells. Colonies of M. orale type 1 and M. orale type 3 adsorbed only chicken red cells. Other mycoplasma species tested, including four of human origin and one of animal origin, did not adsorb red cells or epithelial cells. M. pneumoniae and M. gallisepticum appeared to attach to erythrocytes or tracheal epithelial cells by neuraminic acid receptors on these cells, whereas M. orale types 1 and 3 and M. pulmonis seemed to utilize another type or other types of receptors. Pretreatment of red cells or tracheal epithelial cells with receptor-destroying enzyme, neuraminidase, or influenza B virus removed the adsorption receptors for M. pneumoniae. Similarly, pretreatment of M. pneumoniae colonies with neuraminic acid-containing materials prevented adsorption of erythrocytes or respiratory tract cells. The adsorption sites on M. pneumoniae were specifically blocked by homologous but not heterologous antisera. This property made it possible to study the nature of the mycoplasma adsorption sites by testing the capacity of different fractions of the organism to block the action of adsorption-inhibiting antibodies. Such studies suggested that the mycoplasma binding sites were probably lipid or lipoprotein in nature. The glycerophospholipid hapten was implicated as one such site, since this serologically active hapten blocked the action of hemadsorption-inhibiting antibodies in M. pneumoniae rabbit antiserum. The affinity of M. pneumoniae for respiratory tract epithelium, unique among the mycoplasmas that infect man, may play a role in virulence, since this type of attachment provides an unusual opportunity for peroxide, secreted by the organism, to attack the tissue cell membrane without being rapidly destroyed by catalase or peroxidase present in extracellular body fluids.
D000327:Adsorption; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002645:Chickens; D002850:Chromatography, Gel; D003168:Complement Fixation Tests; D004848:Epithelium; D004912:Erythrocytes / Q000382:microbiology*; D006168:Guinea Pigs; D000882:Haplorhini; D007106:Immune Sera / Q000494:pharmacology; D008055:Lipids / Q000032:analysis; D009174:Mycoplasma / Q000032:analysis / Q000276:immunology; D009438:Neuraminic Acids; D009439:Neuraminidase / Q000494:pharmacology; D009975:Orthomyxoviridae; D010743:Phospholipids / Q000032:analysis; D051381:Rats; D018108:Respirovirus; D014132:Trachea / Q000382:microbiology*; D014357:Trypsin / Q000494:pharmacology; D014774:Virulence; D005719:gamma-Globulins / Q000032:analysis
D007106:Immune Sera; D008055:Lipids; D009438:Neuraminic Acids; D010743:Phospholipids; D005719:gamma-Globulins; D009439:Neuraminidase; D014357:Trypsin