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Legionella effector AnkX interacts with host nuclear protein PLEKHN1

Overview of attention for article published in BMC Microbiology, January 2018
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Title
Legionella effector AnkX interacts with host nuclear protein PLEKHN1
Published in
BMC Microbiology, January 2018
DOI 10.1186/s12866-017-1147-7
Pubmed ID
Authors

Xiaobo Yu, Rebecca R. Noll, Barbara P. Romero Dueñas, Samual C. Allgood, Kristi Barker, Jeffrey L. Caplan, Matthias P. Machner, Joshua LaBaer, Ji Qiu, M. Ramona Neunuebel

Abstract

The intracellular bacterial pathogen Legionella pneumophila proliferates in human alveolar macrophages, resulting in a severe pneumonia termed Legionnaires' disease. Throughout the course of infection, L. pneumophila remains enclosed in a specialized membrane compartment that evades fusion with lysosomes. The pathogen delivers over 300 effector proteins into the host cell, altering host pathways in a manner that sets the stage for efficient pathogen replication. The L. pneumophila effector protein AnkX targets host Rab GTPases and functions in preventing fusion of the Legionella-containing vacuole with lysosomes. However, the current understanding of AnkX's interaction with host proteins and the means through which it exerts its cellular function is limited. Here, we investigated the protein interaction network of AnkX by using the nucleic acid programmable protein array (NAPPA), a high-density platform comprising 10,000 unique human ORFs. This approach facilitated the discovery of PLEKHN1 as a novel interaction partner of AnkX. We confirmed this interaction through multiple independent in vitro pull-down, co-immunoprecipitation, and cell-based assays. Structured illumination microscopy revealed that endogenous PLEKHN1 is found in the nucleus and on vesicular compartments, whereas ectopically produced AnkX co-localized with lipid rafts at the plasma membrane. In mammalian cells, HaloTag-AnkX co-localized with endogenous PLEKHN1 on vesicular compartments. A central fragment of AnkX (amino acids 491-809), containing eight ankyrin repeats, extensively co-localized with endogenous PLEKHN1, indicating that this region may harbor a new function. Further, we found that PLEKHN1 associated with multiple proteins involved in the inflammatory response. Altogether, our study provides evidence that in addition to Rab GTPases, the L. pneumophila effector AnkX targets nuclear host proteins and suggests that AnkX may have novel functions related to manipulating the inflammatory response.

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The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 35 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 35 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 9 26%
Researcher 6 17%
Student > Bachelor 5 14%
Student > Master 4 11%
Professor > Associate Professor 1 3%
Other 1 3%
Unknown 9 26%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 13 37%
Agricultural and Biological Sciences 4 11%
Immunology and Microbiology 3 9%
Engineering 2 6%
Computer Science 1 3%
Other 2 6%
Unknown 10 29%

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 13 February 2018.
All research outputs
#10,007,845
of 12,504,607 outputs
Outputs from BMC Microbiology
#1,262
of 1,841 outputs
Outputs of similar age
#250,170
of 345,234 outputs
Outputs of similar age from BMC Microbiology
#1
of 1 outputs
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