Open AccessThe 40‐ and 90‐kDa membrane proteins (ORF6 gene product) of Mycoplasma pneumoniae are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell
Author(s) -
LayhSchmitt Gerlinde,
Harkenthal Michael
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13561.x
Subject(s) - mycoplasma pneumoniae , gene product , open reading frame , transmembrane protein , biology , mutant , membrane protein , bacterial adhesin , organelle , gene , microbiology and biotechnology , chemistry , biochemistry , membrane , peptide sequence , gene expression , escherichia coli , history , receptor , archaeology , pneumonia
After Triton X‐100 treatment of Mycoplasma pneumoniae cells, a portion of the adhesin P1 (transmembrane protein) proved to remain tightly associated with the Triton insoluble material (Triton shell) as shown previously by several authors. However, the spontaneous loss of two cytadherence‐associated membrane proteins of 90 and 40 kDa (gene product of the open reading frame 6 of the P1 operon) in a hemadsorption‐negative mutant, designated M5, resulted in a 100% release of the P1 protein into the Triton phase and in the lack of the characteristic tip‐like attachment organelle of M. pneumoniae indicating an essential role of the open reading frame 6 gene product in tip structure formation.