Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV

Fadel, Sanaa; Eley, A.

doi:10.1099/jmm.0.2008/001305-0

Cited by 29 publications

(21 citation statements)

References 15 publications

(26 reference statements)

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“…That would also explain why prior exposure to soluble heparin, which is highly sulfated, does not reduce adhesion of C. trachomatis serovar E EBs (13,14,18,19,30,31). Moreover, even heparan sulfate with its heterogeneous and reduced sulfate pattern is unable to block adhesion of C. trachomatis OmcB-E-presenting E. coli cells (32). In contrast, infection by C. trachomatis serovar L2 was inhibited only by the antibody RB4EA12, which recognizes N-sulfated, N-acetylated, and 6-Osulfated regions (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…3A). However, three of them lie immediately C terminal to the single heparin-binding motif (amino acid [aa] 66 to 71; here referred to as the variable domain), and the residues at these positions very likely determine the serovar-specific difference in the heparin dependence of adhesion seen between OmcB proteins from the LGV (OmcB-L) and E (OmcB-E) serovars (12,13,32). Indeed, it has previously been shown that exchange of the variable amino acid at position 66 abrogates the heparin dependency of adhesion by serovar L1 OmcB and, conversely, induces partial heparin dependency of cell binding by serovar E OmcB (13).…”

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confidence: 99%

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Characterization of the Interaction between the Chlamydial Adhesin OmcB and the Human Host Cell

Fechtner¹,

Stallmann²,

Moelleken³

et al. 2013

Journal of Bacteriology

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In a previous study, we reported that the OmcB protein from Chlamydia pneumoniae mediates adhesion of the infectious elementary body to human HEp-2 cells by interacting with heparin/heparan sulfate-like glycosaminoglycans (GAGs) via basic amino acids located in the first of a pair of XBBXBX heparin-binding motifs (K. Moelleken and J. H. Hegemann, Mol. Microbiol. 67:403-419, 2008). In the present study, we show that the basic amino acid at position 57 (arginine) in the first XBBXBX motif, the basic amino acid at position 61 (arginine) in the second motif, and another amino acid (lysine 69) C terminal to it play key roles in the interaction. In addition, we show that discrimination between heparin-dependent and -independent adhesion by C. trachomatis OmcBs is entirely dependent on three variable amino acids in the so-called variable domain C terminal to the conserved XBBXBX motif. Here, the predicted conformational change in the secondary structure induced by the proline at position 66 seems to be crucial for heparin recognition. Finally, we performed neutralization experiments using different anti-heparan sulfate antibodies to gain insight into the nature of the GAGs recognized by OmcB. The results suggest that C. trachomatis serovar L2 OmcB interacts with 6-O-sulfated domains of heparan sulfate, while C. pneumoniae OmcB apparently interacts with domains of heparan sulfate harboring a diverse subset of O-sulfations.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Characterization of the Interaction between the Chlamydial Adhesin OmcB and the Human Host Cell

Fechtner¹,

Stallmann²,

Moelleken³

et al. 2013

Journal of Bacteriology

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“…Furthermore, FGF2 enhances binding of Chlamydia in an heparan sulfate proteoglycan-dependent manner (37). Candidate Chlamydia proteins involved in these interactions include the Chlamydia OmcB protein, which binds to glycosaminoglycans, such as heparan sulfate (38)(39)(40).…”

Section: Discussionmentioning

confidence: 99%

Attachment ofChlamydia trachomatisL2 to host cells requires sulfation

Rosmarin

Carette

Olive

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Chlamydia trachomatis is a pathogen responsible for a prevalent sexually transmitted disease. It is also the most common cause of infectious blindness in the developing world. We performed a loss-of-function genetic screen in human haploid cells to identify host factors important in C. trachomatis L2 infection. We identified and confirmed B3GAT3 , B4GALT7 , and SLC35B2 , which encode glucuronosyltransferase I, galactosyltransferase I, and the 3′-phosphoadenosine 5′-phosphosulfate transporter 1, respectively, as important in facilitating Chlamydia infection. Knockout of any of these three genes inhibits Chlamydia attachment. In complementation studies, we found that the introduction of functional copies of these three genes into the null clones restored full susceptibility to Chlamydia infection. The degree of attachment of Chlamydia strongly correlates with the level of sulfation of the host cell, not simply with the amount of heparan sulfate. Thus, other, as-yet unidentified sulfated macromolecules must contribute to infection. These results demonstrate the utility of screens in haploid cells to study interactions of human cells with bacteria. Furthermore, the human null clones generated can be used to investigate the role of heparan sulfate and sulfation in other settings not limited to infectious disease.

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“…LGVl and E show GAG-dependent and independent binding to host cells, respectively, indicating that it may be involved in either the primary or secondary attachment step [114]. C. pneumoniae Pmp proteins contain tetrapeptide repeat motifs that mediate binding to epithelial cells, and a recent study indicates that the presence of multiple Pmps have an additive effect on attachment to host cells [115].…”

Section: Type III Secretionmentioning

confidence: 99%

“…LGVI but not E prevents EBs from binding [114] host cells. [111 ] mAb reduces C.trachomatis L2 binding.…”

Section: L2mentioning

confidence: 99%

Identification and biochemical characterization of the CHLAMYDIA TRACHOMATIS type III secretion chaperone, SLC1, and its role in the translocation of the invasion-associated effector TARP.

Brinkworth¹

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Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV

Cited by 29 publications

References 15 publications

Characterization of the Interaction between the Chlamydial Adhesin OmcB and the Human Host Cell

Characterization of the Interaction between the Chlamydial Adhesin OmcB and the Human Host Cell

Attachment ofChlamydia trachomatisL2 to host cells requires sulfation

Identification and biochemical characterization of the CHLAMYDIA TRACHOMATIS type III secretion chaperone, SLC1, and its role in the translocation of the invasion-associated effector TARP.

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