scholarly journals Characterization of Cell Wall Polymers Secreted into the Growth Medium of Lysis-Defective Pneumococci During Treatment with Penicillin and Other Inhibitors of Cell Wall Synthesis

1978 ◽  
Vol 13 (2) ◽  
pp. 302-311 ◽  
Author(s):  
R. Hakenbeck ◽  
S. Waks ◽  
A. Tomasz
Keyword(s):  
Cell Wall ◽  
Growth Medium ◽  
Cell Wall Synthesis ◽  
Cell Wall Polymers

Cloning and Characterization of psu1+, a New Essential Fission Yeast Gene Involved in Cell Wall Synthesis

1999 ◽  
Vol 262 (2) ◽  
pp. 368-374 ◽  
Author(s):  
Kazuo Omi ◽  
Hikaru Sonoda ◽  
Kiyoshi Nagata ◽  
Kenji Sugita
Keyword(s):  
Cell Wall ◽  
Fission Yeast ◽  
Cell Wall Synthesis ◽  
Yeast Gene

Rotational-Echo Double Resonance Characterization of the Effects of Vancomycin on Cell Wall Synthesis inStaphylococcus aureus†

Biochemistry ◽  
2002 ◽  
Vol 41 (43) ◽  
pp. 13053-13058 ◽  
Author(s):  
Lynette Cegelski ◽  
Sung Joon Kim ◽  
Andrew W. Hing ◽  
Daniel R. Studelska ◽  
Robert D. O'Connor ◽  
...  
Keyword(s):  
Cell Wall ◽  
Double Resonance ◽  
Cell Wall Synthesis ◽  
Rotational Echo Double Resonance

scholarly journals Characterization of the Aspergillus fumigatus phosphomannose isomerase Pmi1 and its impact on cell wall synthesis and morphogenesis

Microbiology ◽  
2009 ◽  
Vol 155 (10) ◽  
pp. 3281-3293 ◽  
Author(s):  
Wenxia Fang ◽  
Xiaoying Yu ◽  
Bin Wang ◽  
Hui Zhou ◽  
Haomiao Ouyang ◽  
...  
Keyword(s):  
Cell Wall ◽  
Aspergillus Fumigatus ◽  
Energy Production ◽  
Mutant Cell ◽  
Phosphomannose Isomerase ◽  
Cell Wall Synthesis ◽  
High Concentration ◽  
Human Fungal Pathogen ◽  
Sugar Chains

Phosphomannose isomerase (PMI) is an enzyme catalysing the interconversion of mannose 6-phosphate (Man-6-P) and fructose 6-phosphate (Fru-6-P). The reaction catalysed by PMI is the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation. In this study, the pmi1 gene was identified to encode PMI in the human fungal pathogen Aspergillus fumigatus. Characterization of A. fumigatus Pmi1 expressed in Escherichia coli revealed that this PMI mainly catalysed the conversion of Fru-6-P to Man-6-P and that its binding affinity for Man-6-P was similar to that of yeast PMIs, but different to those of PMIs from bacteria or animals. Loss of pmi1 was lethal unless Man was provided in the growth medium. However, a Δpmi1 mutant cell showed a significantly reduced growth rate at a high concentration of Man. Biochemical analysis revealed that both inadequate and replete Man led to an accumulation of intracellular Man-6-P and a reduction in the amount of α-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene led to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation. Our results reveal that PMI activity is essential for viability and plays a central regulatory role in both cell wall synthesis and energy production in A. fumigatus.

scholarly journals GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis

2019 ◽  
Author(s):  
Jeanine Rismondo ◽  
Talal F. M. Haddad ◽  
Yang Shen ◽  
Martin J. Loessner ◽  
Angelika Gründling
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Listeria Monocytogenes ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Wall Teichoic Acid ◽  
Gram Positive Bacteria ◽  
Cell Wall Polymers ◽  
Galactose Residue

ABSTRACTThe cell wall polymers wall teichoic acid (WTA) and lipoteichoic acid (LTA) are often modified with glycosyl and D-alanine residues. Recent studies have shown that a three-component glycosylation system is used for the modification of LTA in several Gram-positive bacteria including Bacillus subtilis and Listeria monocytogenes. In the L. monocytogenes 1/2a strain 10403S, the cytoplasmic glycosyltransferase GtlA is thought to use UDP-galactose to produce the C55-P-galactose lipid intermediate, which is transported across the membrane by an unknown flippase. Next, the galactose residue is transferred onto the LTA backbone on the outside of the cell by the glycosyltransferase GtlB. Here we show that GtcA is necessary for the glycosylation of LTA in L. monocytogenes 10403S and B. subtilis 168 and we hypothesize that these proteins act as C55-P-sugar flippases. With this we revealed that GtcA is involved in the glycosylation of both teichoic acid polymers in L. monocytogenes 10403S, namely WTA with N-acetylglucosamine and LTA with galactose residues. These findings indicate that the L. monocytogenes GtcA protein can act on different C55-P-sugar intermediates. Further characterization of GtcA in L. monocytogenes led to the identification of residues essential for its overall function as well as residues, which predominately impact WTA or LTA glycosylation.GRAPHICAL ABSTRACT

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