Download Chlamydia pneumoniae : infection and disease by Herman Friedman, Yoshimasa Yamamoto, Mauro Bendinelli PDF

By Herman Friedman, Yoshimasa Yamamoto, Mauro Bendinelli

Chlamydia pneumoniae is a micro organism that's most typically recognized for inflicting colds and pneumonia. although, researchers have lately discovered a hyperlink among C. pneumoniae and atherosclerosis, a clogging of the arteries that factors middle assault and stroke. additionally, ongoing examine is displaying that definite traces may possibly play a job in bronchial asthma, a number of sclerosis, Alzheimer's ailment, and arthritis.

This quantity, a part of the Infectious brokers and Pathogenesis sequence, is a whole portrait of C. pneumoniae and what's at the moment recognized approximately it.

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Extra resources for Chlamydia pneumoniae : infection and disease

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28) identified YscC in C. pneumoniae COMC proteome, but not YscL, YscN, and LcrE, the other Type III secretion system proteins identified in EB. These proteins are supposed to be localized in the chlamydial cytosol, the inner membrane, and in contact with the host cells (Fig. 2). There is no direct evidence for the protrusions to be constituted by the type III gene products but it is likely that they are. Since these are found to penetrate through the inclusion membrane it is likely that they are providing contact with the outer of the inclusion.

Periplasmic space Omp2 is seen connected to Omp3. The structure of COMC is complex, with LPS, Ppm, spike-like structures, and MOMP trimers being surface exposed. 5. CHLAMYDIA GENOMES Sequencing of Chlamydia genomes has provided new means to analyze the molecular and structural biology of Chlamydia. There are now published five complete genome sequences: for C. trachomatis D,(18) C. trachomatis MoPn,(19) and C. (19) Chlamydia is, the microbe with most sequenced genomes. This has greatly expanded the information concerning the biology of these obligate intracellular pathogens.

Outer membrane when stained negatively because of penetration of the staining solution into the outer membranes, indicating that the whole inner layer of EB outer membrane is composed of HAS (Fig. 6). To determine the periodicity of the HAS, the computer Fourier transformation was applied to outer membranes stained negatively (Fig. 7). The result obtained demonstrated that the EB outer membrane was composed of three structural units with dimensions of 176, 90 and 50 Å respectively. When an image was reconstituted using only spots showing 176 Å periodicity by the inverse Fourier transformation, a distinct HAS image was obtained (Fig.

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