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Proteomic Analysis of the Ehrlichia chaffeensis Phagosome in Cultured DH82 Cells

Overview of attention for article published in PLOS ONE, February 2014
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Title
Proteomic Analysis of the Ehrlichia chaffeensis Phagosome in Cultured DH82 Cells
Published in
PLOS ONE, February 2014
DOI 10.1371/journal.pone.0088461
Pubmed ID
Authors

Yan Cheng, Yan Liu, Bin Wu, Jian-zhi Zhang, Jiang Gu, Ya-ling Liao, Fu-kun Wang, Xu-hu Mao, Xue-jie Yu

Abstract

Ehrlichia chaffeensis is an obligately intracellular bacterium that resides and multiplies within cytoplasmic vacuoles of phagocytes. The Ehrlichia-containing vacuole (ECV) does not fuse with lysosomes, an essential condition for Ehrlichia to survive inside phagocytes, but the mechanism of inhibiting the fusion of the phagosome with lysosomes is not clear. Understanding the ECV molecular composition may decipher the mechanism by which Ehrlichia inhibits phagosome-lysosome fusion. In this study, we obtained highly purified ECVs from E. chaffeensis-infected DH82 cells by sucrose density gradient centrifugation and analyzed their composition by mass spectrometry-based proteomics. The ECV composition was compared with that of phagolysosomes containing latex beads. Lysosomal proteins such as cathepsin D, cathepsin S, and lysosomal acid phosphatase were not detected in E. chaffeensis phagosome preparations. Some small GTPases, involved in membrane dynamics and phagocytic trafficking, were detected in ECVs. A notable finding was that Rab7, a late endosomal marker, was consistently detected in E. chaffeensis phagosomes by mass spectrometry. Confocal microscopy confirmed that E. chaffeensis phagosomes contained Rab7 and were acidified at approximately pH 5.2, suggesting that the E. chaffeensis vacuole was an acidified late endosomal compartment. Our results also demonstrated by mass spectrometry and immunofluorescence analysis that Ehrlichia morulae were not associated with the autophagic pathway. Ehrlichia chaffeensis did not inhibit phagosomes containing latex beads from fusing with lysosomes in infected cells. We concluded that the E. chaffeensis vacuole was a late endosome and E. chaffeensis might inhibit phagosome-lysosome fusion by modifying its vacuolar membrane composition, rather than by regulating the expression of host genes involved in trafficking.

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Mendeley readers

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Geographical breakdown

Country Count As %
Brazil 1 3%
Unknown 29 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 6 20%
Student > Master 5 17%
Student > Bachelor 5 17%
Researcher 4 13%
Professor > Associate Professor 3 10%
Other 1 3%
Unknown 6 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 7 23%
Veterinary Science and Veterinary Medicine 4 13%
Medicine and Dentistry 4 13%
Immunology and Microbiology 4 13%
Biochemistry, Genetics and Molecular Biology 3 10%
Other 2 7%
Unknown 6 20%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 24 February 2014.
All research outputs
#18,369,403
of 22,751,628 outputs
Outputs from PLOS ONE
#154,398
of 194,172 outputs
Outputs of similar age
#163,635
of 223,893 outputs
Outputs of similar age from PLOS ONE
#4,401
of 5,782 outputs
Altmetric has tracked 22,751,628 research outputs across all sources so far. This one is in the 11th percentile – i.e., 11% of other outputs scored the same or lower than it.
So far Altmetric has tracked 194,172 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 15.1. This one is in the 10th percentile – i.e., 10% of its peers scored the same or lower than it.
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