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Anne Marie Di Guilmi
Researcher at University of Grenoble
Publications - 44
Citations - 2116
Anne Marie Di Guilmi is an academic researcher from University of Grenoble. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 28, co-authored 41 publications receiving 1980 citations. Previous affiliations of Anne Marie Di Guilmi include French Alternative Energies and Atomic Energy Commission & Joseph Fourier University.
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Journal ArticleDOI
The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae
Maxime Jacq,Maxime Jacq,Christopher Arthaud,Sylvie Manuse,Sylvie Manuse,Chryslène Mercy,Laure Bellard,Katharina Peters,Benoit Gallet,Jennifer Galindo,Thierry Doan,Waldemar Vollmer,Yves V. Brun,Michael S. VanNieuwenhze,Anne Marie Di Guilmi,Thierry Vernet,Christophe Grangeasse,Cécile Morlot +17 more
TL;DR: It is shown that the putative lysozyme activity of the cell wall hydrolase Pmp23 is important for proper morphology and cell division in the opportunistic human pathogen Streptococcus pneumoniae and a new regulatory function for peptidoglycan hydrolases is revealed.
Journal ArticleDOI
Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae.
J. Bonnet,Claire Durmort,Maxime Jacq,Isabelle Mortier-Barrière,Nathalie Campo,Michael S. VanNieuwenhze,Yves V. Brun,Christopher Arthaud,Benoit Gallet,Christine Moriscot,Cécile Morlot,Thierry Vernet,Anne Marie Di Guilmi +12 more
TL;DR: It is shown that O‐acetylation driven by Adr protects the peptidoglycan of dividing cells from cleavage by the major autolysin LytA and occurs at the septal site.
Journal ArticleDOI
Nanoscale Dynamics of Peptidoglycan Assembly During the Cell Cycle of Streptococcus pneumoniae
Jennyfer Trouve,André Zapun,Christopher Arthaud,Claire Durmort,Anne Marie Di Guilmi,Bill Soederstroem,Christophe Grangeasse,Dominique Bourgeois,Yung-Sing Wong,Cécile Morlot +9 more
TL;DR: N nanoscale-resolution data reveal spatio-temporal features of peptidoglycan assembly and fate along the cell cycle and provide geometrical parameters that were used to construct a morphogenesis model of the ovoid cell.
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Structural studies of the transpeptidase domain of PBP1a from Streptococcus pneumoniae
TL;DR: To initiate the determination of the three-dimensional structure of a class A PBP, crystals of the transpeptidase domain of PBP1a from Streptococcus pneumoniae were prepared by limited proteolysis of the full-length molecule and purification by anion-exchange chromatography and gel filtration.
Journal ArticleDOI
Structure of the choline-binding domain of Spr1274 in Streptococcus pneumoniae.
Zhenyi Zhang,Wenzhe Li,Cecile Frolet,Rui Bao,Anne Marie Di Guilmi,Thierry Vernet,Yuxing Chen +6 more
TL;DR: The crystal structure of the choline-binding domain of Spr1274 (residues 44-129) was solved at 2.38 A resolution with three molecules in the asymmetric unit and may provide a structural basis for functional analysis of ch Caroline-binding proteins.