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AmiD Is a Novel Peptidoglycan Amidase in Wolbachia Endosymbionts of Drosophila melanogaster

Identifieur interne : 000793 ( Main/Exploration ); précédent : 000792; suivant : 000794

AmiD Is a Novel Peptidoglycan Amidase in Wolbachia Endosymbionts of Drosophila melanogaster

Auteurs : Miriam Wilmes [Allemagne] ; Kirstin Meier [Allemagne] ; Andrea Schiefer [Allemagne] ; Michaele Josten [Allemagne] ; Christian F. Otten [Royaume-Uni] ; Anna Klöckner [Allemagne] ; Beate Henrichfreise [Allemagne] ; Waldemar Vollmer [Royaume-Uni] ; Achim Hoerauf [Allemagne] ; Kenneth Pfarr [Allemagne]

Source :

RBID : PMC:5543032

Abstract

Wolbachia endobacteria are obligate intracellular bacteria with a highly reduced genome infecting many arthropod and filarial species, in which they manipulate arthropod reproduction to increase their transmission and are essential for nematode development and survival. The Wolbachia genome encodes all enzymes required for the synthesis of the cell wall building block lipid II, although a peptidoglycan-like structure has not been detected. Despite the ability to synthesize lipid II, Wolbachia from arthropods and nematodes have only a subset of genes encoding enzymes involved in the periplasmic processing of lipid II and peptidoglycan recycling, with arthropods having two more than nematodes. We functionally analyzed the activity of the putative cell wall hydrolase AmiD from the Wolbachia endosymbiont of Drosophila melanogaster, an enzyme not encoded by the nematode endobacteria. Wolbachia AmiD has Zn2+-dependent amidase activity and cleaves intact peptidoglycan, monomeric lipid II and anhydromuropeptides, substrates that are generated during bacterial growth. AmiD may have been maintained in arthropod Wolbachia to avoid host immune recognition by degrading cell wall fragments in the periplasm. This is the first description of a wolbachial lipid II processing enzyme putatively expressed in the periplasm.


Url:
DOI: 10.3389/fcimb.2017.00353
PubMed: 28824885
PubMed Central: 5543032


Affiliations:


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<italic>Wolbachia</italic>
endobacteria are obligate intracellular bacteria with a highly reduced genome infecting many arthropod and filarial species, in which they manipulate arthropod reproduction to increase their transmission and are essential for nematode development and survival. The
<italic>Wolbachia</italic>
genome encodes all enzymes required for the synthesis of the cell wall building block lipid II, although a peptidoglycan-like structure has not been detected. Despite the ability to synthesize lipid II,
<italic>Wolbachia</italic>
from arthropods and nematodes have only a subset of genes encoding enzymes involved in the periplasmic processing of lipid II and peptidoglycan recycling, with arthropods having two more than nematodes. We functionally analyzed the activity of the putative cell wall hydrolase AmiD from the
<italic>Wolbachia</italic>
endosymbiont of
<italic>Drosophila melanogaster</italic>
, an enzyme not encoded by the nematode endobacteria.
<italic>Wolbachia</italic>
AmiD has Zn
<sup>2+</sup>
-dependent amidase activity and cleaves intact peptidoglycan, monomeric lipid II and anhydromuropeptides, substrates that are generated during bacterial growth. AmiD may have been maintained in arthropod
<italic>Wolbachia</italic>
to avoid host immune recognition by degrading cell wall fragments in the periplasm. This is the first description of a wolbachial lipid II processing enzyme putatively expressed in the periplasm.</p>
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<name sortKey="Hoerauf, Achim" sort="Hoerauf, Achim" uniqKey="Hoerauf A" first="Achim" last="Hoerauf">Achim Hoerauf</name>
<name sortKey="Josten, Michaele" sort="Josten, Michaele" uniqKey="Josten M" first="Michaele" last="Josten">Michaele Josten</name>
<name sortKey="Klockner, Anna" sort="Klockner, Anna" uniqKey="Klockner A" first="Anna" last="Klöckner">Anna Klöckner</name>
<name sortKey="Meier, Kirstin" sort="Meier, Kirstin" uniqKey="Meier K" first="Kirstin" last="Meier">Kirstin Meier</name>
<name sortKey="Pfarr, Kenneth" sort="Pfarr, Kenneth" uniqKey="Pfarr K" first="Kenneth" last="Pfarr">Kenneth Pfarr</name>
<name sortKey="Schiefer, Andrea" sort="Schiefer, Andrea" uniqKey="Schiefer A" first="Andrea" last="Schiefer">Andrea Schiefer</name>
</country>
<country name="Royaume-Uni">
<noRegion>
<name sortKey="Otten, Christian F" sort="Otten, Christian F" uniqKey="Otten C" first="Christian F." last="Otten">Christian F. Otten</name>
</noRegion>
<name sortKey="Vollmer, Waldemar" sort="Vollmer, Waldemar" uniqKey="Vollmer W" first="Waldemar" last="Vollmer">Waldemar Vollmer</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/LymphedemaV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000793 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000793 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Sante
   |area=    LymphedemaV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     PMC:5543032
   |texte=   AmiD Is a Novel Peptidoglycan Amidase in Wolbachia Endosymbionts of Drosophila melanogaster
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:28824885" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a LymphedemaV1 

Wicri

This area was generated with Dilib version V0.6.31.
Data generation: Sat Nov 4 17:40:35 2017. Site generation: Tue Feb 13 16:42:16 2024