Adhesion and biofilm formation of Mycoplasma pneumoniae on an abiotic surface

Kornspan, David; Tarshis, Mark; Rottem, Shlomo

doi:10.1007/s00203-011-0749-y

Cited by 29 publications

(19 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…M. pneumoniae may tightly adsorb onto the surface of the host cells, depending on the specific adhesion structure, to avoid phagocytosis prior to exact antibody adjustment (65). The polymorphism of M. pneumoniae adhesion antigens also weakens the effects of specific antibodies (66). The glycerophosphatide on M. pneumoniae cell membranes shares certain antigenic components with the host cells, and thus can also evade the host's immune surveillance.…”

Section: Antigen Immune Damagementioning

confidence: 99%

Insights into the pathogenesis of Mycoplasma pneumoniae

Liu

et al. 2016

Molecular Medicine Reports

View full text Add to dashboard Cite

Mycoplasma are the smallest prokaryotic microbes present in nature. These wall-less, malleable organisms can pass through cell filters, and grow and propagate under cell-free conditions in vitro. Of the pathogenic Mycoplasma Mycoplasma pneumoniae has been examined the most. In addition to primary atypical pneumonia and community-acquired pneumonia with predominantly respiratory symptoms, M. pneumoniae can also induce autoimmune hemolytic anemia and other diseases in the blood, cardiovascular system, gastrointestinal tract and skin, and can induce pericarditis, myocarditis, nephritis and meningitis. The pathogenesis of M. pneumoniae infection is complex and remains to be fully elucidated. The present review aimed to summarize several direct damage mechanisms, including adhesion damage, destruction of membrane fusion, nutrition depletion, invasive damage, toxic damage, inflammatory damage and immune damage. Further investigations are required for determining the detailed pathogenesis of M. pneumoniae.

show abstract

Section: Antigen Immune Damagementioning

confidence: 99%

Insights into the pathogenesis of Mycoplasma pneumoniae

Liu

et al. 2016

Molecular Medicine Reports

View full text Add to dashboard Cite

show abstract

“…Finally, heparin has also been implicated in biofilm formation by increasing cell-cell interactions in the Gram-positive pathogens, S. aureus 127 and Lactobacillus rhamnosus 128 . M. pneumoniae forms large, complex biofilms on abiotic surfaces 34 . Heparin affinity chromatography of M. pneumoniae has been performed previously 129 identifying only nine proteins, none of which was P1.…”

Section: Discussionmentioning

confidence: 99%

Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules

Widjaja

Berry

Jarocki

et al. 2020

Sci Rep

View full text Add to dashboard Cite

Mycoplasma pneumoniae is a genome reduced pathogen and causative agent of community acquired pneumonia. The major cellular adhesin, P1, localises to the tip of the attachment organelle forming a complex with P40 and P90, two cleavage fragments derived by processing Mpn142, and other molecules with adhesive and mobility functions. LC-MS/MS analysis of M. pneumoniae M129 proteins derived from whole cell lysates and eluents from affinity matrices coupled with chemically diverse host molecules identified 22 proteoforms of P1. Terminomics was used to characterise 17 cleavage events many of which were independently verified by the identification of semitryptic peptides in our proteome studies and by immunoblotting. One cleavage event released 1597 tSAAKpGApRppVppKpGApKppVQppKKpA 1627 from the C-terminus of P1 and this peptide was shown to bind to a range of host molecules. A smaller synthetic peptide comprising the C-terminal 15 amino acids, 1613 pGApKppVQppKKpA 1627 , selectively bound cytoskeletal intermediate filament proteins cytokeratin 7, cytokeratin 8, cytokeratin 18, and vimentin from a native A549 cell lysate. Collectively, our data suggests that ectodomain shedding occurs on the surface of M. pneumoniae where it may alter the functional diversity of P1, Mpn142 and other surface proteins such as elongation factor Tu via a mechanism similar to that described in Mycoplasma hyopneumoniae. The attachment organelle is a structurally and functionally sophisticated component of the M. pneumoniae cell that is responsible for the assembly of proteins essential for motility and adherence 1-8. An extensive list of host molecules including fibronectin 9-13 , fibrinogen 10-14 , plasminogen 11-13,15-17 , lactoferrin 10-12 , laminin 10-12 , and vitronectin 10-13 interact with surface accessible adhesins in M. pneumoniae. Other less well-defined host molecules include sialylated molecules 18 , oligosaccharides 19 , glycolipids 20 , and glycoproteins 21. The gene mpn141 encoding the major adhesin P1 is located in the same operon along with mpn140 and mpn142 and these three genes constitute a polycistronic transcriptional unit 22,23. mpn140 encodes for a 28 kDa putative phosphoesterase 24 and while it has been shown to degrade nanoRNA and dephosphorylate 3′-phosphoadenosine 5′-phosphate to AMP 25 , no role in adherence has been assigned for this protein. mpn142 generates a 130 kDa product (Mpn142) that is cleaved into two fragments of 40 kDa (P40) and 90 kDa (P90) immediately after or concurrent with translation 26,27. The cleavage event in Mpn142, first described over 25 years ago, was the first in what is now known to be a highly processed molecule on the surface of M. pneumoniae 28. P1 is a remarkably versatile molecule and the subject of numerous studies over the past 30 years. The only cleavage event that has been accurately assigned to P1 is the removal of the N-terminal 59 amino acids as a leader peptide 29. Molecular cross-linking and immunogold-labelling studies indicated that P1 forms a complex with P30, P40, and P90 ...

show abstract

“…It is generally accepted that most infectious diseases are caused by pathogens that have the capacity to form biofilms (Donlan, 2001). Many species of mycoplasma including Mycoplasma pneumoniae form biofilms (García-Castillo et al, 2008;Kornspan et al, 2011;McAuliffe et al, 2006;. This wall-less pathogen has a significant impact on human health, causing atypical pneumonia and accounting for 100 000 hospitalizations in the United States annually .…”

Section: Introductionmentioning

confidence: 99%

Type 1 and type 2 strains of Mycoplasma pneumoniae form different biofilms

et al. 2013

View full text Add to dashboard Cite

Several mycoplasma species have been shown to form biofilms that confer resistance to antimicrobials and which may affect the host immune system, thus making treatment and eradication of the pathogens difficult. The present study shows that the biofilms formed by two strains of the human pathogen Mycoplasma pneumoniae differ quantitatively and qualitatively. Compared with strain UAB PO1, strain M129 grows well but forms biofilms that are less robust, with towers that are less smooth at the margins. A polysaccharide containing Nacetylglucosamine is secreted by M129 into the culture medium but found in tight association with the cells of UAB PO1. The polysaccharide may have a role in biofilm formation, contributing to differences in virulence, chronicity and treatment outcome between strains of M. pneumoniae. The UAB PO1 genome was found to be that of a type 2 strain of M. pneumoniae, whereas M129 is type 1. Examination of other M. pneumoniae isolates suggests that the robustness of the biofilm correlates with the strain type.

show abstract

Adhesion and biofilm formation of Mycoplasma pneumoniae on an abiotic surface

Cited by 29 publications

References 13 publications

Insights into the pathogenesis of Mycoplasma pneumoniae

Insights into the pathogenesis of Mycoplasma pneumoniae

Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules

Type 1 and type 2 strains of Mycoplasma pneumoniae form different biofilms

Contact Info

Product

Resources

About