Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm

Manli Qi, Lei Lei, Siqi Gong, Quanzhong Liu, Matthew P. DeLisa, Guangming Zhong

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The Chlamydia-specific hypothetical protein CT795 was dominantly recognized by human antisera produced during C. trachomatis infection but not by animal antisera raised against dead chlamydia organisms. The immundominant region recognized by the human antibodies was mapped to the N-terminal fragment T22-S69. The endogenous CT795 was detected in the cytoplasm of host cells during C. trachomatis infection and was highly enriched in the host cytosolic fraction but absent in the purified chlamydia organisms, suggesting that CT795 is synthesized and secreted into host cell cytoplasm without incorporation into the organisms. All C. trachomatis serovars tested secreted CT795. A predicted signal peptide of CT795 directed the mature PhoA to cross Escherichia coli inner membranes. The secretion of CT795 in Chlamydia-infected cells was inhibited by a C16compound targeting signal peptidase I, but not by a C1 compound known to block the type III secretion pathway. These results suggest that CT795, like CPAF (a Chlamydia-secreted virulence factor), is secreted into the host cell cytoplasm via a sec-dependent mechanism and not by a type III secretion pathway. The above characterizations of CT795 have provided important information for further understanding the potential roles of CT795 in C. trachomatis pathogenesis.

Original languageEnglish (US)
Pages (from-to)2498-2509
Number of pages12
JournalJournal of Bacteriology
Volume193
Issue number10
DOIs
StatePublished - May 2011

Fingerprint

Chlamydia
Chlamydia trachomatis
Cytoplasm
Chlamydia Infections
Secretory Pathway
Proteins
Immune Sera
Virulence Factors
Protein Sorting Signals
Escherichia coli
Membranes
Antibodies

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm. / Qi, Manli; Lei, Lei; Gong, Siqi; Liu, Quanzhong; DeLisa, Matthew P.; Zhong, Guangming.

In: Journal of Bacteriology, Vol. 193, No. 10, 05.2011, p. 2498-2509.

Research output: Contribution to journalArticle

Qi, Manli ; Lei, Lei ; Gong, Siqi ; Liu, Quanzhong ; DeLisa, Matthew P. ; Zhong, Guangming. / Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm. In: Journal of Bacteriology. 2011 ; Vol. 193, No. 10. pp. 2498-2509.
@article{b411cc8751ff452fb5696bff02445c71,
title = "Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm",
abstract = "The Chlamydia-specific hypothetical protein CT795 was dominantly recognized by human antisera produced during C. trachomatis infection but not by animal antisera raised against dead chlamydia organisms. The immundominant region recognized by the human antibodies was mapped to the N-terminal fragment T22-S69. The endogenous CT795 was detected in the cytoplasm of host cells during C. trachomatis infection and was highly enriched in the host cytosolic fraction but absent in the purified chlamydia organisms, suggesting that CT795 is synthesized and secreted into host cell cytoplasm without incorporation into the organisms. All C. trachomatis serovars tested secreted CT795. A predicted signal peptide of CT795 directed the mature PhoA to cross Escherichia coli inner membranes. The secretion of CT795 in Chlamydia-infected cells was inhibited by a C16compound targeting signal peptidase I, but not by a C1 compound known to block the type III secretion pathway. These results suggest that CT795, like CPAF (a Chlamydia-secreted virulence factor), is secreted into the host cell cytoplasm via a sec-dependent mechanism and not by a type III secretion pathway. The above characterizations of CT795 have provided important information for further understanding the potential roles of CT795 in C. trachomatis pathogenesis.",
author = "Manli Qi and Lei Lei and Siqi Gong and Quanzhong Liu and DeLisa, {Matthew P.} and Guangming Zhong",
year = "2011",
month = "5",
doi = "10.1128/JB.01301-10",
language = "English (US)",
volume = "193",
pages = "2498--2509",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "10",

}

TY - JOUR

T1 - Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm

AU - Qi, Manli

AU - Lei, Lei

AU - Gong, Siqi

AU - Liu, Quanzhong

AU - DeLisa, Matthew P.

AU - Zhong, Guangming

PY - 2011/5

Y1 - 2011/5

N2 - The Chlamydia-specific hypothetical protein CT795 was dominantly recognized by human antisera produced during C. trachomatis infection but not by animal antisera raised against dead chlamydia organisms. The immundominant region recognized by the human antibodies was mapped to the N-terminal fragment T22-S69. The endogenous CT795 was detected in the cytoplasm of host cells during C. trachomatis infection and was highly enriched in the host cytosolic fraction but absent in the purified chlamydia organisms, suggesting that CT795 is synthesized and secreted into host cell cytoplasm without incorporation into the organisms. All C. trachomatis serovars tested secreted CT795. A predicted signal peptide of CT795 directed the mature PhoA to cross Escherichia coli inner membranes. The secretion of CT795 in Chlamydia-infected cells was inhibited by a C16compound targeting signal peptidase I, but not by a C1 compound known to block the type III secretion pathway. These results suggest that CT795, like CPAF (a Chlamydia-secreted virulence factor), is secreted into the host cell cytoplasm via a sec-dependent mechanism and not by a type III secretion pathway. The above characterizations of CT795 have provided important information for further understanding the potential roles of CT795 in C. trachomatis pathogenesis.

AB - The Chlamydia-specific hypothetical protein CT795 was dominantly recognized by human antisera produced during C. trachomatis infection but not by animal antisera raised against dead chlamydia organisms. The immundominant region recognized by the human antibodies was mapped to the N-terminal fragment T22-S69. The endogenous CT795 was detected in the cytoplasm of host cells during C. trachomatis infection and was highly enriched in the host cytosolic fraction but absent in the purified chlamydia organisms, suggesting that CT795 is synthesized and secreted into host cell cytoplasm without incorporation into the organisms. All C. trachomatis serovars tested secreted CT795. A predicted signal peptide of CT795 directed the mature PhoA to cross Escherichia coli inner membranes. The secretion of CT795 in Chlamydia-infected cells was inhibited by a C16compound targeting signal peptidase I, but not by a C1 compound known to block the type III secretion pathway. These results suggest that CT795, like CPAF (a Chlamydia-secreted virulence factor), is secreted into the host cell cytoplasm via a sec-dependent mechanism and not by a type III secretion pathway. The above characterizations of CT795 have provided important information for further understanding the potential roles of CT795 in C. trachomatis pathogenesis.

UR - http://www.scopus.com/inward/record.url?scp=79956141341&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79956141341&partnerID=8YFLogxK

U2 - 10.1128/JB.01301-10

DO - 10.1128/JB.01301-10

M3 - Article

C2 - 21441519

AN - SCOPUS:79956141341

VL - 193

SP - 2498

EP - 2509

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 10

ER -