<i>Chlamydia trachomatis</i>
            IncA Is Localized to the Inclusion Membrane and Is Recognized by Antisera from Infected Humans and Primates

Bannantine, John P.; Stamm, Walter E.; Suchland, Robert J.; Rockey, Daniel D.

doi:10.1128/iai.66.12.6017-6021.1998

Cited by 82 publications

(41 citation statements)

References 23 publications

(21 reference statements)

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“…Comparison of hydropathy pro®les for the predicted amino acid sequences of known inclusion membrane proteins. Each of these proteins has been localized to the chlamydial inclusion membrane using¯uorescence microscopy with speci®c antibody either previously Bannantine et al, 1998aBannantine et al, , 1998b or in this report (C. pneumoniae IncA). Pro®les were determined using the algorithm developed by Kyte and Doolittle (1982) with a window size of seven amino acids.…”

Section: Selection Of C-incs For Production Of Antiseramentioning

confidence: 56%

“…Chlamydia psittaci IncA and IncC were initially detected by sera from C. psittaci-infected guinea pigs Bannantine et al, 1998a). Chlamydia trachomatis IncA is also recognized by a majority of sera from C. trachomatis-infected humans as well as experimentally infected primates (Bannantine et al, 1998b). Antibodies to linear Inc protein epitopes are not, however, universal.…”

Section: Discussionmentioning

confidence: 99%

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A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane

et al. 2000

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Chlamydiae are obligate intracellular pathogens that spend their entire growth phase sequestered in a membrane-bound vacuole called an inclusion. A set of chlamydial proteins, labelled Inc proteins, has been identified in the inclusion membrane (IM). The predicted IncA, IncB and IncC amino acid sequences share very limited similarity, but a common hydrophobicity motif is present within each Inc protein. In an effort to identify a relatively complete catalogue of Chlamydia trachomatis proteins present in the IM of infected cells, we have screened the genome for open reading frames encoding this structural motif. Hydropathy plot analysis was used to screen each translated open reading frame in the C. trachomatis genome database. Forty-six candidate IM proteins (C-lncs) that satisfied the criteria of containing a bilobed hydrophobic domain of at least 50 amino acids were identified. The genome of Chlamydia pneumoniae encodes a larger collection of C-lnc proteins, and only approximately half of the C-lncs are encoded within both genomes. In order to confirm the hydropathy plot screening method as a valid predictor of C-lncs, antisera and/or monoclonal antibodies were prepared against six of the C. trachomatis C-lncs. Immunofluorescence microscopy of C. trachomatis-infected cells probed with these antibodies showed that five out of six C-lncs are present in the chlamydial IM. Antisera were also produced against C. pneumoniae p186, a protein sharing identity with Chlamydia psittaci lncA and carrying a similar bilobed hydrophobic domain. These antisera labelled the inclusion membrane in C. pneumoniae infected cells, confirming that proteins sharing the unique secondary structural characteristic also localize to the inclusion membrane of C. pneumoniae. Sera from patients with high-titre antibodies to C. trachomatis were examined for reactivity with each tested C-lnc protein. Three out of six tested C-lncs were recognized by a majority of these patient sera. Collectively, these studies identify and characterize novel proteins localized to the chlamydial IM and demonstrate the existence of a potential secondary structural targeting motif for localization of chlamydial proteins to this unique intracellular environment.

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Section: Selection Of C-incs For Production Of Antiseramentioning

confidence: 56%

Section: Discussionmentioning

confidence: 99%

A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane

et al. 2000

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“…Again, these proteins were present uniquely in Chlamydia-infected cells, but not in puri®ed EBs and uninfected cells. Although the function of these proteins is unknown, they may be involved in nutrient acquisition and in pathogen±host interaction (Bannantine et al, 1998b).…”

Section: Discussionmentioning

confidence: 99%

Characterization and intracellular trafficking pattern of vacuoles containing Chlamydia pneumoniae in human epithelial cells

1999

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SummaryChlamydiae are obligate intracellular pathogens that reside within a membrane-bound vacuole throughout their developmental cycle. In this study, the intraphagosomal pH of Chlamydia pneumoniae (Cpn) was qualitatively assessed, and the intracellular fate of the pathogen-containing vacuole and its interaction with endocytic organelles in human epithelial cells were analysed using conventional immuno¯uores-cence and confocal microscopy. The pH-sensitive probes acridine orange (AO), LysoTracker (LyT) and DAMP did not accumulate in the bacterial inclusion. In addition, exposure of cells to ba®lomycin A1 (BafA1), a potent acidi®cation inhibitor, did not inhibit or delay chlamydial growth. The chlamydial compartment was not accessible to the¯uid-phase tracer Texas Red (TR)-dextran and did not exhibit any level of staining for the late endosomal marker cation-independent mannose-6-phosphate receptor (Ci-M6PR) or for the lysosomal-associated membrane proteins (LAMP-1 and -2) and CD63. In addition, transferrin receptor (TfR)-enriched vesicles were observed close to Cpn vacuoles, potentially indicating a speci®c translocation of these organelles through the cytoplasm to the vicinity of the vacuole. We conclude that Cpn, like other chlamydial spp., circumvents the host endocytic pathway and inhabits a non-acidic vacuole, which is dissociated from late endosomes and lysosomes, but selectively accumulates early endosomes.

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“…Using the characteristic hydropathy profile, in silico searching for these proteins led to the prediction of 90 candidates in C. pneumoniae J138 and 36 in C. trachomatis serovar D [57]. Inc proteins, were originally identified in C. psittaci, and subsequently found in C. trachomatis [58]. IncA was experimentally proven to be an inclusion membrane protein by intracellular reactivity of the protein following microinjection of fluorescent antibody into infected cells [59].…”

Section: Inclusion Modificationmentioning

confidence: 99%

The chlamydial developmental cycle: Figure 1

AbdelRahman¹,

Belland²

2005

FEMS Microbiol Rev

530

478

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Intracellular parasitism by bacterial pathogens is a complex, multi-factorial process that has been exploited successfully by a wide variety of organisms. Members of the Order Chlamydiales are obligate intracellular bacteria that are transmitted as metabolically inactive particles and must differentiate, replicate, and re-differentiate within the host cell to carry out their life cycle. Understanding the developmental cycle has been greatly advanced by the availability of complete genome sequences, DNA microarrays, and advanced cell biology techniques. Measuring transcriptional changes throughout the cycle has allowed investigators to determine the nature of the temporal gene expression changes required for bacterial growth and development.

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Chlamydia trachomatis IncA Is Localized to the Inclusion Membrane and Is Recognized by Antisera from Infected Humans and Primates

Cited by 82 publications

References 23 publications

A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane

A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane

Characterization and intracellular trafficking pattern of vacuoles containing Chlamydia pneumoniae in human epithelial cells

The chlamydial developmental cycle: Figure 1

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