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Title: Characterization of the structure and catalytic activity of Legionella pneumophila VipF: L. pneumophila VipF Modifies Chloramphenicol

Authors:
 [1];  [1];  [1];  [1]; ORCiD logo [1]
  1. Department of Chemistry and Biochemistry, James Madison University, Harrisonburg Virginia 22807
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1401692
Grant/Contract Number:
AC02-06CH11357
Resource Type:
Journal Article: Publisher's Accepted Manuscript
Journal Name:
Proteins
Additional Journal Information:
Journal Volume: 84; Journal Issue: 10; Related Information: CHORUS Timestamp: 2017-10-20 17:56:36; Journal ID: ISSN 0887-3585
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
United States
Language:
English

Citation Formats

Young, Byron H., Caldwell, Tracy A., McKenzie, Aidan M., Kokhan, Oleksandr, and Berndsen, Christopher E. Characterization of the structure and catalytic activity of Legionella pneumophila VipF: L. pneumophila VipF Modifies Chloramphenicol. United States: N. p., 2016. Web. doi:10.1002/prot.25087.
Young, Byron H., Caldwell, Tracy A., McKenzie, Aidan M., Kokhan, Oleksandr, & Berndsen, Christopher E. Characterization of the structure and catalytic activity of Legionella pneumophila VipF: L. pneumophila VipF Modifies Chloramphenicol. United States. doi:10.1002/prot.25087.
Young, Byron H., Caldwell, Tracy A., McKenzie, Aidan M., Kokhan, Oleksandr, and Berndsen, Christopher E. 2016. "Characterization of the structure and catalytic activity of Legionella pneumophila VipF: L. pneumophila VipF Modifies Chloramphenicol". United States. doi:10.1002/prot.25087.
@article{osti_1401692,
title = {Characterization of the structure and catalytic activity of Legionella pneumophila VipF: L. pneumophila VipF Modifies Chloramphenicol},
author = {Young, Byron H. and Caldwell, Tracy A. and McKenzie, Aidan M. and Kokhan, Oleksandr and Berndsen, Christopher E.},
abstractNote = {},
doi = {10.1002/prot.25087},
journal = {Proteins},
number = 10,
volume = 84,
place = {United States},
year = 2016,
month = 7
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1002/prot.25087

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  • Pathogens deliver complex arsenals of translocated effector proteins to host cells during infection, but the extent to which these proteins are regulated once inside the eukaryotic cell remains poorly defined. Among all bacterial pathogens, Legionella pneumophila maintains the largest known set of translocated substrates, delivering over 300 proteins to the host cell via its Type IVB, Icm/Dot translocation system. Backed by a few notable examples of effector–effector regulation in L. pneumophila, we sought to define the extent of this phenomenon through a systematic analysis of effector–effector functional interaction. We used Saccharomyces cerevisiae, an established proxy for the eukaryotic host, tomore » query > 108,000 pairwise genetic interactions between two compatible expression libraries of ~330 L. pneumophila–translocated substrates. While capturing all known examples of effector–effector suppression, we identify fourteen novel translocated substrates that suppress the activity of other bacterial effectors and one pair with synergistic activities. In at least nine instances, this regulation is direct—a hallmark of an emerging class of proteins called metaeffectors, or “effectors of effectors”. Through detailed structural and functional analysis, we show that metaeffector activity derives from a diverse range of mechanisms, shapes evolution, and can be used to reveal important aspects of each cognate effector's function. Here, metaeffectors, along with other, indirect, forms of effector–effector modulation, may be a common feature of many intracellular pathogens—with unrealized potential to inform our understanding of how pathogens regulate their interactions with the host cell.« less
  • A 31-kilodalton (kDa) protein was solubilized from the peptidoglycan (PG) fraction of Legionella pneumophila after treatment with either N-acetylmuramidase from the fungus Chalaropsis sp. or with mutanolysin from Streptomyces globisporus. The protein exhibited a ladderlike banding pattern by autoradiography when radiolabeled ((35S)cysteine or (35S)methionine) PG material was extensively treated with hen lysozyme. The banding patterns ranging between 31 and 45 kDa and between 55 and 60 kDa resolved as a single 31-kDa protein when the material was subsequently treated with N-acetylmuramidase. Analysis of the purified 31-kDa protein for diaminopimelic acid by gas chromatography revealed 1 mol of diaminopimelic acid permore » mol of protein. When outer membrane PG material containing the major outer membrane porin protein was treated with N-acetylmuramidase or mutanolysin, both the 28.5-kDa major outer membrane protein and the 31-kDa protein were solubilized from the PG material under reducing conditions. In the absence of 2-mercaptoethanol, a high-molecular-mass complex (100 kDa) was resolved. The results of this study indicate that a 31-kDa PG-bound protein is a major component of the cell wall of L. pneumophila whose function may be to anchor the major outer membrane protein to PG. Finally, a survey of other Legionella species and other serogroups of L. pneumophila suggested that PG-bound proteins may be a common feature of this genus.« less
  • Cited by 4
  • Cited by 4