Chlamydial Adhesion and Adhesins

Hegemann, Johannes H.; Moelleken, Katja

doi:10.1128/9781555817329.ch5

Cited by 15 publications

(23 citation statements)

References 141 publications

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“…Structure prediction programs have indicated that the passenger domains of Pmps are dominated by parallel ␤-strands disposed in a helical pattern with three faces that form a ␤-helix (17,18). It has, therefore, been speculated that these ␤-helices could associate with each other to generate Pmp oligomers (20).…”

Section: Discussionmentioning

confidence: 99%

“…11 and 14) can interact with each other to form heteromeric protofibrils. If so, this would provide for greater antigenic complexity and enable Chlamydiae to adapt to a larger range of cellular niches (14,20).…”

Section: Discussionmentioning

confidence: 99%

“…␤-Helical structures are a characteristic of autotransporters and might be required for their efficient translocation across the outer membrane and for folding (19). Moreover, it has been speculated that Pmp ␤-helices could associate with each other to generate oligomers (20). Like other autotransporter proteins, many Pmps undergo complex proteolytic processing (13,18,(21)(22)(23)(24).…”

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confidence: 99%

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The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties

Luczak

Smits²,

Decker

et al. 2016

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties

Luczak

Smits²,

Decker

et al. 2016

Journal of Biological Chemistry

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“…The diversity in binding and internalization mechanisms between species probably contributes to differences in tropism for specific hosts and tissues. The adhesion of C. trachomatis , C. pneumoniae and C. muridarum is a two-step process that is mediated by a low-affinity interaction with heparan sulfate proteoglycans (HSPGs) followed by high-affinity binding to host cell receptors 17 . OmcB (also known as CT443) from C. trachomatis L1 or C. pneumoniae mediates attachment to HSPGs 17 .…”

Section: Binding and Invasionmentioning

confidence: 99%

“…The adhesion of C. trachomatis , C. pneumoniae and C. muridarum is a two-step process that is mediated by a low-affinity interaction with heparan sulfate proteoglycans (HSPGs) followed by high-affinity binding to host cell receptors 17 . OmcB (also known as CT443) from C. trachomatis L1 or C. pneumoniae mediates attachment to HSPGs 17 . The level and position of sulfation in HSPGs have important roles in the binding of C. muridarum and C. trachomatis L2 (REFS 17,28,29) and may contribute to tissue tropism.…”

Section: Binding and Invasionmentioning

confidence: 99%

Chlamydia cell biology and pathogenesis

2016

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Chlamydia spp. are important causes of human disease for which no effective vaccine exists. These obligate intracellular pathogens replicate in a specialized membrane compartment and use a large arsenal of secreted effectors to survive in the hostile intracellular environment of the host. In this Review, we summarize the progress in decoding the interactions between Chlamydia spp. and their hosts that has been made possible by recent technological advances in chlamydial proteomics and genetics. The field is now poised to decipher the molecular mechanisms that underlie the intimate interactions between Chlamydia spp. and their hosts, which will open up many exciting avenues of research for these medically important pathogens.

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All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species‐specific function

Becker

Hegemann

2014

MicrobiologyOpen

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The bacterial pathogens Chlamydia trachomatis and C. pneumoniae are obligate intracellular parasites, cause a number of serious diseases, and can infect various cell types in humans. Chlamydial infections are probably initiated by binding of the bacterial outer membrane protein OmcB to host cell glycosaminoglycans (GAGs). Here, we show that all nine members of the polymorphic membrane protein (Pmp) family of C. trachomatis mediate adhesion to human epithelial and endothelial cells. Importantly, exposure of infectious particles to soluble recombinant Pmps blocks subsequent infection, thus implicating an important function of the entire protein family in the infection process. Analogous experiments with pairs of recombinant Pmps or a combination of Pmp and OmcB revealed that all Pmps probably act in an adhesion pathway that is distinct from the OmcB-GAG pathway. Finally, we provide evidence that the Pmps of C. trachomatis and C. pneumoniae exhibit species and tissue specificity. These findings argue for the involvement of C. trachomatis Pmps in the initial phase of infection and suggest that they may interact with a receptor other than the epidermal growth factor receptor recently identified for their counterparts in C. pneumoniae.

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Chlamydial Adhesion and Adhesins

Cited by 15 publications

References 141 publications

The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties

The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties

Chlamydia cell biology and pathogenesis

All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species‐specific function

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