The 40- and 90-kDa membrane proteins (ORF6 gene product) of<i>Mycoplasma pneumoniae</i>are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell

Layh‐Schmitt, Gerlinde; Harkenthal, M

doi:10.1111/j.1574-6968.1999.tb13561.x

Cited by 31 publications

(9 citation statements)

References 26 publications

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“…However, the lack of the ORF6 gene product in a spontaneous haemadsorption-negative mutant resulted in the release of all the P1 protein into the Triton-soluble phase (Layh-Schmitt & Harkenthal, 1999). These findings suggest that the ORF6 gene product may be responsible for proper disposition of the P1 molecules in the mycoplasma membrane, which seems to be a prerequisite for interaction of the 40 and 90 kDa cytadherence-associated proteins and the P1 protein with the cytoskeleton.…”

Section: Introductionmentioning

confidence: 72%

“…The results indicate that clustering of the P1 adhesin together with the adhesin-related 30 kDa protein and the cytadherence accessory proteins of 40 and 90 kDa in the membrane of the characteristic terminal structure of the cell is essential for effective attachment of M. pneumoniae to its host cell. The 40 and 90 kDa proteins and the cytoskeleton-forming proteins HMW1-HMW3 are required for tip structure formation and clustering of the P1 protein in the tip, as spontaneous cytadherence-negative mutants lacking the 40 and 90 kDa protein or HMW1-HMW3 exhibit a round or ovoid morphology without a distinct terminal organelle (Baseman et al, 1982 ;Hahn et al, 1998 ;Layh-Schmitt et al, 1995 ;Layh-Schmitt & Harkenthal, 1999). Moreover, these mutations resulted in a random distribution of the P1 protein in the mycoplasma cell membranes, suggesting an intimate interaction of the P1 protein, not only with the 40 and 90 kDa proteins, but also with one or more of the HMW1-HMW3 proteins.…”

Section: Discussionmentioning

confidence: 99%

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Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae

Layh‐Schmitt

Podtelejnikov²,

Mann³

2000

Microbiology

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Adherence of Mycoplasma pneumoniae to host cells requires several mycoplasmal membrane proteins and cytoskeleton-like proteins in addition to the adhesin P1, a transmembrane protein of 170 kDa. To analyse interactions of the P1 adhesin with other membrane proteins or with cytoskeleton-like proteins, cross-linking studies were performed in vivo using the permeant reagent paraformaldehyde. The cross-linked protein complex was isolated by immunoaffinity chromatography, and proteins complexed to the P1 protein were identified by immunoblot analysis followed by high mass accuracy tryptic peptide mapping using matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). In addition to the P1 protein and a truncated form of the same protein, the adhesin-related 30 kDa protein, two membrane proteins of 40 and 90 kDa, the cytoskeleton-associated 65 kDa protein and two cytoskeleton-forming proteins, HMW1 and HMW3, were found to be components of the isolated protein complex. Furthermore, the cross-linked complex contained the chaperone DnaK and the E1α subunit of pyruvate dehydrogenase. In summary, it was shown that cytadherence-associated membrane proteins are located in close proximity to cytoskeleton-like proteins, suggesting a functional interaction between membrane and cytoskeleton-like proteins. DnaK might be involved in translocation of proteins from the cytoplasm to the membrane and pyruvate dehydrogenase might be a structural protein of the attachment organelle.

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Section: Introductionmentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae

Layh‐Schmitt

Podtelejnikov²,

Mann³

2000

Microbiology

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“…Our electron microscopy studies revealed that the typical flask-shaped appearance of M. gallisepticum , presenting a defined single knob-like structure at one polar end, changed to a rounder, bulkier morphology, with less defined tip structures in strains lacking GapA and CrmA. Similarly, M. pneumoniae mutant M5 which had lost the homolog of CrmA exhibits a perfect round cell shape, but has lost the tip-like structure [ 53 ]. Mutants of M. pneumoniae lacking homologs of GapA and CrmA also have lost the elongated flask-shape and display a branched cell morphology [ 54 ].…”

Section: Discussionmentioning

confidence: 99%

First identification of proteins involved in motility of Mycoplasma gallisepticum

Indikova

Vronka

Szostak

2014

Vet Res

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Mycoplasma gallisepticum, the most pathogenic mycoplasma in poultry, is able to glide over solid surfaces. Although this gliding motility was first observed in 1968, no specific protein has yet been shown to be involved in gliding. We examined M. gallisepticum strains and clonal variants for motility and found that the cytadherence proteins GapA and CrmA were required for gliding. Loss of GapA or CrmA resulted in the loss of motility and hemadsorption and led to drastic changes in the characteristic flask-shape of the cells. To identify further genes involved in motility, a transposon mutant library of M. gallisepticum was generated and screened for motility-deficient mutants, using a screening assay based on colony morphology. Motility-deficient mutants had transposon insertions in gapA and the neighbouring downstream gene crmA. In addition, insertions were seen in gene mgc2, immediately upstream of gapA, in two motility-deficient mutants. In contrast to the GapA/CrmA mutants, the mgc2 motility mutants still possessed the ability to hemadsorb. Complementation of these mutants with a mgc2-hexahistidine fusion gene restored the motile phenotype. This is the first report assigning specific M. gallisepticum proteins to involvement in gliding motility.

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“…Insertion of P1 into the membrane and its trafficking to the attachment organelle is largely dependent on P90 and P40 [38,39,40]. Mutants defective in the expression of P90 and P40 allow P1 to completely partition to the Triton X-100 soluble phase.…”

Section: Introductionmentioning

confidence: 99%

“…Mutants defective in the expression of P90 and P40 allow P1 to completely partition to the Triton X-100 soluble phase. In wild type cells, P1 typically partially associates with the Triton X-100 insoluble shell [39]. Mutants unable to produce mpn142 are defective in cellular adherence because P1 cannot traffic to the tip structure resulting in random P1 distribution around the cell body [38,40].…”

Section: Introductionmentioning

confidence: 99%

P40 and P90 from Mpn142 are Targets of Multiple Processing Events on the Surface of Mycoplasma pneumoniae

et al. 2015

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Mycoplasma pneumoniae is a significant cause of community acquired pneumonia globally. Despite having a genome less than 1 Mb in size, M. pneumoniae presents a structurally sophisticated attachment organelle that (i) provides cell polarity, (ii) directs adherence to receptors presented on respiratory epithelium, and (iii) plays a major role in cell motility. The major adhesins, P1 (Mpn141) and P30 (Mpn453), are localised to the tip of the attachment organelle by the surface accessible cleavage fragments P90 and P40 derived from Mpn142. Two events play a defining role in the formation of P90 and P40; removal of a leader peptide at position 26 (23SLA↓NTY28) during secretion to the cell surface and cleavage at amino acid 455 (452GPL↓RAG457) generating P40 and P90. Liquid Chromatography Tandem Mass Spectrometry (LC-MS/MS) analysis of tryptic peptides generated by digesting size-fractionated cell lysates of M. pneumoniae identified 15 cleavage fragments of Mpn142 ranging in mass from 9–84 kDa. Further evidence for the existence of cleavage fragments of Mpn142 was generated by mapping tryptic peptides to proteins recovered from size fractionated eluents from affinity columns loaded with heparin, fibronectin, fetuin, actin, plasminogen and A549 surface proteins as bait. To define the sites of cleavage in Mpn142, neo-N-termini in cell lysates of M. pneumoniae were dimethyl-labelled and characterised by LC-MS/MS. Our data suggests that Mpn142 is cleaved to generate adhesins that are auxiliary to P1 and P30.

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The 40- and 90-kDa membrane proteins (ORF6 gene product) ofMycoplasma pneumoniaeare responsible for the tip structure formation and P1 (adhesin) association with the Triton shell

Cited by 31 publications

References 26 publications

Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae

Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae

First identification of proteins involved in motility of Mycoplasma gallisepticum

P40 and P90 from Mpn142 are Targets of Multiple Processing Events on the Surface of Mycoplasma pneumoniae

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