Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm

Lei Lei, Manli Qi, Nicole Budrys, Robert S Schenken, Guangming Zhong

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The chlamydia-specific hypothetical protein CT311 was detected both inside and outside of the chlamydial inclusions in Chlamydia trachomatis-infected cells. The extra-inclusion CT311 molecules were distributed in the host cell cytoplasm with a pattern similar to that of CPAF, a known Chlamydia-secreted protease. The detection of CT311 was specific since the anti-CT311 antibody labeling was only removed by absorption with CT311 but not CPAF fusion proteins. In addition, both anti-CT311 and anti-CPAF antibodies only detected their corresponding endogenous proteins without cross-reacting with each other or any other antigens in the whole cell lysates of C. trachomatis-infected cells. Although both CT311 and CPAF proteins were first detected 12 h after infection, localization of CT311 into host cell cytosol was delayed until 24 h while CPAF secretion into host cell cytosol was already obvious by 18 h after infection. The host cell cytosolic localization of CT311 was further confirmed in human primary cells. CT311 was predicted to contain an N-terminal secretion signal sequence and the CT311 signal sequence directed secretion of PhoA into bacterial periplasmic region in a heterologous assay system, suggesting that a sec-dependent pathway may play a role in the secretion of CT311 into host cell cytosol. This hypothesis is further supported by the observation that secretion of CT311 in Chlamydia-infected cells was blocked by a C16 compound known to inhibit signal peptidase I. These findings have provided important molecular information for further understanding the C. trachomatis pathogenic mechanisms.

Original languageEnglish (US)
Pages (from-to)101-109
Number of pages9
JournalMicrobial Pathogenesis
Volume51
Issue number3
DOIs
StatePublished - Sep 2011

Fingerprint

Chlamydia trachomatis
Cytoplasm
Proteins
Chlamydia
Cytosol
Protein Sorting Signals
Anti-Idiotypic Antibodies
Infection
Peptide Hydrolases
Antigens

Keywords

  • Chlamydia trachomatis
  • Hypothetical CT311
  • Secretion

ASJC Scopus subject areas

  • Microbiology
  • Infectious Diseases

Cite this

Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm. / Lei, Lei; Qi, Manli; Budrys, Nicole; Schenken, Robert S; Zhong, Guangming.

In: Microbial Pathogenesis, Vol. 51, No. 3, 09.2011, p. 101-109.

Research output: Contribution to journalArticle

@article{802e1d34914a485ba8e9c191e23a19e0,
title = "Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm",
abstract = "The chlamydia-specific hypothetical protein CT311 was detected both inside and outside of the chlamydial inclusions in Chlamydia trachomatis-infected cells. The extra-inclusion CT311 molecules were distributed in the host cell cytoplasm with a pattern similar to that of CPAF, a known Chlamydia-secreted protease. The detection of CT311 was specific since the anti-CT311 antibody labeling was only removed by absorption with CT311 but not CPAF fusion proteins. In addition, both anti-CT311 and anti-CPAF antibodies only detected their corresponding endogenous proteins without cross-reacting with each other or any other antigens in the whole cell lysates of C. trachomatis-infected cells. Although both CT311 and CPAF proteins were first detected 12 h after infection, localization of CT311 into host cell cytosol was delayed until 24 h while CPAF secretion into host cell cytosol was already obvious by 18 h after infection. The host cell cytosolic localization of CT311 was further confirmed in human primary cells. CT311 was predicted to contain an N-terminal secretion signal sequence and the CT311 signal sequence directed secretion of PhoA into bacterial periplasmic region in a heterologous assay system, suggesting that a sec-dependent pathway may play a role in the secretion of CT311 into host cell cytosol. This hypothesis is further supported by the observation that secretion of CT311 in Chlamydia-infected cells was blocked by a C16 compound known to inhibit signal peptidase I. These findings have provided important molecular information for further understanding the C. trachomatis pathogenic mechanisms.",
keywords = "Chlamydia trachomatis, Hypothetical CT311, Secretion",
author = "Lei Lei and Manli Qi and Nicole Budrys and Schenken, {Robert S} and Guangming Zhong",
year = "2011",
month = "9",
doi = "10.1016/j.micpath.2011.05.002",
language = "English (US)",
volume = "51",
pages = "101--109",
journal = "Microbial Pathogenesis",
issn = "0882-4010",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm

AU - Lei, Lei

AU - Qi, Manli

AU - Budrys, Nicole

AU - Schenken, Robert S

AU - Zhong, Guangming

PY - 2011/9

Y1 - 2011/9

N2 - The chlamydia-specific hypothetical protein CT311 was detected both inside and outside of the chlamydial inclusions in Chlamydia trachomatis-infected cells. The extra-inclusion CT311 molecules were distributed in the host cell cytoplasm with a pattern similar to that of CPAF, a known Chlamydia-secreted protease. The detection of CT311 was specific since the anti-CT311 antibody labeling was only removed by absorption with CT311 but not CPAF fusion proteins. In addition, both anti-CT311 and anti-CPAF antibodies only detected their corresponding endogenous proteins without cross-reacting with each other or any other antigens in the whole cell lysates of C. trachomatis-infected cells. Although both CT311 and CPAF proteins were first detected 12 h after infection, localization of CT311 into host cell cytosol was delayed until 24 h while CPAF secretion into host cell cytosol was already obvious by 18 h after infection. The host cell cytosolic localization of CT311 was further confirmed in human primary cells. CT311 was predicted to contain an N-terminal secretion signal sequence and the CT311 signal sequence directed secretion of PhoA into bacterial periplasmic region in a heterologous assay system, suggesting that a sec-dependent pathway may play a role in the secretion of CT311 into host cell cytosol. This hypothesis is further supported by the observation that secretion of CT311 in Chlamydia-infected cells was blocked by a C16 compound known to inhibit signal peptidase I. These findings have provided important molecular information for further understanding the C. trachomatis pathogenic mechanisms.

AB - The chlamydia-specific hypothetical protein CT311 was detected both inside and outside of the chlamydial inclusions in Chlamydia trachomatis-infected cells. The extra-inclusion CT311 molecules were distributed in the host cell cytoplasm with a pattern similar to that of CPAF, a known Chlamydia-secreted protease. The detection of CT311 was specific since the anti-CT311 antibody labeling was only removed by absorption with CT311 but not CPAF fusion proteins. In addition, both anti-CT311 and anti-CPAF antibodies only detected their corresponding endogenous proteins without cross-reacting with each other or any other antigens in the whole cell lysates of C. trachomatis-infected cells. Although both CT311 and CPAF proteins were first detected 12 h after infection, localization of CT311 into host cell cytosol was delayed until 24 h while CPAF secretion into host cell cytosol was already obvious by 18 h after infection. The host cell cytosolic localization of CT311 was further confirmed in human primary cells. CT311 was predicted to contain an N-terminal secretion signal sequence and the CT311 signal sequence directed secretion of PhoA into bacterial periplasmic region in a heterologous assay system, suggesting that a sec-dependent pathway may play a role in the secretion of CT311 into host cell cytosol. This hypothesis is further supported by the observation that secretion of CT311 in Chlamydia-infected cells was blocked by a C16 compound known to inhibit signal peptidase I. These findings have provided important molecular information for further understanding the C. trachomatis pathogenic mechanisms.

KW - Chlamydia trachomatis

KW - Hypothetical CT311

KW - Secretion

UR - http://www.scopus.com/inward/record.url?scp=79959350828&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79959350828&partnerID=8YFLogxK

U2 - 10.1016/j.micpath.2011.05.002

DO - 10.1016/j.micpath.2011.05.002

M3 - Article

C2 - 21605656

AN - SCOPUS:79959350828

VL - 51

SP - 101

EP - 109

JO - Microbial Pathogenesis

JF - Microbial Pathogenesis

SN - 0882-4010

IS - 3

ER -