Cryo-electron tomography of Chlamydia trachomatis gives a clue to the mechanism of outer membrane changes

Journal of Electron Microscopy

Volumn 59, Issue 3, 2010, Pages 237-241

  Huang, Zengwei ^a   Chen, Mukai ^b   Li, Kunpeng ^a   Dong, Xiaoduo ^a   Han, Jiande ^b   Zhang, Qinfen ^a  

^a Attardi Institute of Mitochondrial Biomedicine   (China)

^b SUN YAT SEN UNIVERSITY   (China)

Author keywords

Chlamydia trachomatis; Cryo electron tomography; Inner membrane; Outer membrane

Indexed keywords

OUTER MEMBRANE PROTEIN;

ARTICLE; CHLAMYDIA TRACHOMATIS; CRYOELECTRON MICROSCOPY; ELECTRON TOMOGRAPHY; HUMAN; METABOLISM; METHODOLOGY; ULTRASTRUCTURE;

BACTERIAL OUTER MEMBRANE PROTEINS; CHLAMYDIA TRACHOMATIS; CRYOELECTRON MICROSCOPY; ELECTRON MICROSCOPE TOMOGRAPHY; HUMANS;

CHLAMYDIA TRACHOMATIS;

ELECTRIC IMPEDANCE TOMOGRAPHY;

CHLAMYDIA TRACHOMATIS; CRYO-ELECTRON TOMOGRAPHY; INNER MEMBRANES; OUTER MEMBRANE; ULTRA-THIN;

MEMBRANES;

EID: 77953247793     PISSN: 00220744     EISSN: 14779986     Source Type: Journal    
DOI: 10.1093/jmicro/dfp057     Document Type: Article

References (17)

1. Abdelrahman Y M and Belland R J (2005) The chlamydial developmental cycle. FEMS Microbiol. Rev. 29: 949-959.
2. Hogan R J, Mathews S A, Mukhopadhyay S, Summersgill J T, and Timms P (2004) Chlamydial persistence: beyond the biphasic paradigm. Infect Immun. 72: 1843-1855.
3. Koning R I and Koster A J (2009) Cryo-electron tomography in biology and medicine. Ann Anat. 191: 427-445.
4. Mayer J, Woods M L, Vavrin Z, and Hibbs J B (1993) Gamma interferon-induced nitric oxide production reduces Chlamydia trachomatis infectivity in McCoy cells. Infect Immun. 61: 491-497.
5. Kremer J R,Mastronarde D N, andMc ntosh J R (1996) Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116: 71-76.
6. Frangakis A S and Hegerl R (2001) Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 135: 239-250.
7. Ludtke S J, Baldwin P R, and Chiu W (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128: 82-97.
8. Pettersen E F, Goddard T D, Huang C C, Couch G S, Greenblatt D M, Meng E C, and Ferrin T E (2004) UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25: 1605-1612.
9. Matsumoto A (1982) Surface projections of Chlamydia psittaci elementary bodies as revealed by freeze-deep-etching. J. Bacteriol. 151: 1040-1042. (Pubitemid 12027998)
10. Nichols B A, Setzer P Y, Pang F, and Dawson C R (1985) New view of the surface projections of Chlamydia trachomatis. J. Bacteriol. 164: 344-349.
11. Everett K D and Hatch T P (1991) Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC. J. Bacteriol. 173: 3821-3830.
12. Hatch T P, Allan I, and Pearce J H (1984) Structural and polypeptide differences between envelopes of infective and reproductive life cycle forms of Chlamydia spp. J. Bacteriol. 157: 13-20.
13. Newhall W J T (1987) Biosynthesis and disulfide cross-linking of outer membrane components during the growth cycle of Chlamydia trachomatis. Infect Immun. 55: 162-168.
14. Sardinia L M, Segal E, and Ganem D (1988) Developmental regulation of the cysteine-rich outer-membrane proteins of murine Chlamydia trachomatis. J. Gen Microbiol. 134: 997-1004.
15. Lambden P R, Everson J S,WardME, and Clarke I N (1990) Sulfur-rich proteins of Chlamydia trachomatis: developmentally regulated transcription of polycistronic mRNA from tandem promoters. Gene. 87: 105-112.
16. Hatch T P (1996) Disulfide cross-linked envelope proteins: the functional equivalent of peptidoglycan in chlamydiae? J. Bacteriol. 178: 1-5.
17. Everett K D and Hatch T P (1995) Architecture of the cell envelope of Chlamydia psittaci 6BC. J. Bacteriol. 177: 877-882.