Phospholipids of
            <i>Streptococcus faecalis</i>

Mota, J. M. dos Santos; Kamp, J.A.F. Op den; Verheij, Hubertus M.; Deenen, L.L.M. Van

doi:10.1128/jb.104.2.611-619.1970

Cited by 44 publications

(1 citation statement)

References 47 publications

(33 reference statements)

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“…Yet E. faecalis does not produce the variety of phospholipids found in many bacterial species. To date, it is known only to produce phosphatidylglycerol and two derivatives, lysyl-phosphatidylglycerol and cardiolipin ( 2 – 5 ). Glucosyl-lipids are also produced which can result in the formation of lipoteichoic acid.…”

Section: Commentarymentioning

confidence: 99%

Too Much or Not Enough: The Role of mprF in Regulating Overall Phospholipid Content

Fozo

2023

mBio

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Despite their fundamental role in defining cells, lipids and the contributions of specific lipid classes in bacterial physiology and pathogenesis have not been highlighted well. Enterococcus faecalis , a commensal bacterial and major hospital-acquired bacterium, synthesizes only a few known phospholipids. One of these variants, lysyl-phosphatidylglycerol, is critical for surviving cationic antimicrobial peptides, but its consequence on overall membrane composition and cellular properties has not been thoroughly examined.

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Section: Commentarymentioning

confidence: 99%

Too Much or Not Enough: The Role of mprF in Regulating Overall Phospholipid Content

Fozo

2023

mBio

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Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol

Roy

2009

IUBMB Life

116

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SummaryThe bacterial envelope is a semi-permeable barrier that protects the cell from the hostilities of the environment. To survive the ever-changing conditions of their surroundings, bacteria need to rapidly adjust the biochemical properties of their cellular envelope. Amino acid (aa) addition to phosphatidylglycerol (PG) of the membrane is one of the mechanisms used by bacteria to lower the net negative charge of their cellular envelope, thereby decreasing its affinity for several antibacterial agents such as the cationic antimicrobial peptides (CAMPs) produced by the innate immune response during host infection. This process requires the activity of an integral membrane protein, called aa-PG synthase (aaPGS), to transfer the aa of aminoacyltRNA (aa-tRNA) onto the PG of the membrane. aaPGSs constitute a new family of virulence factors that are found in a wide range of microorganisms. aa-PGs not only provide resistance to CAMPs but also to other classes of antibacterial agents and to environmental stresses such as those encountered during extreme osmotic or acidic conditions. This review will describe the known biochemical properties of aa-PGSs, their specificity for aa-tRNAs and phospholipids, and the growing repertoire of aa used as substrates by these enzymes. Their prevalence in bacteria and the phenotypes and modulations of membrane properties associated with these molecules will be addressed, as well as their regulation as a component of the envelope stress response system in certain bacteria.

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Roles of tRNA in cell wall biosynthesis

Dare

Ibba

2012

WIREs RNA

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Recent research into various aspects of bacterial metabolism such as cell wall and antibiotic synthesis, degradation pathways, cellular stress, and amino acid biosynthesis has elucidated roles of aminoacyl-transfer ribonucleic acid (aa-tRNA) outside of translation. Although the two enzyme families responsible for cell wall modifications, aminoacyl-phosphatidylglycerol synthases (aaPGSs) and Fem, were discovered some time ago, they have recently become of intense interest for their roles in the antimicrobial resistance of pathogenic microorganisms. The addition of positively charged amino acids to phosphatidylglycerol (PG) by aaPGSs neutralizes the lipid bilayer making the bacteria less susceptible to positively charged antimicrobial agents. Fem transferases utilize aa-tRNA to form peptide bridges that link strands of peptidoglycan. These bridges vary among the bacterial species in which they are present and play a role in resistance to antibiotics that target the cell wall. Additionally, the formation of truncated peptides results in shorter peptide bridges and loss of branched linkages which makes bacteria more susceptible to antimicrobials. A greater understanding of the structure and substrate specificity of this diverse enzymatic family is necessary to aid current efforts in designing potential bactericidal agents. These two enzyme families are linked only by the substrate with which they modify the cell wall, aa-tRNA; their structure, cell wall modification processes and the physiological changes they impart on the bacterium differ greatly.

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Phospholipids of Streptococcus faecalis

Cited by 44 publications

References 47 publications

Too Much or Not Enough: The Role of mprF in Regulating Overall Phospholipid Content

Too Much or Not Enough: The Role of mprF in Regulating Overall Phospholipid Content

Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol

Roles of tRNA in cell wall biosynthesis

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