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A partial reconstitution implicates DltD in catalyzing lipoteichoic acid d-alanylation.

B McKay Wood¹, John P Santa Maria¹, Leigh M Matano¹

¹From the Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.

The Journal of Biological Chemistry

|September 22, 2018

Summary

The d-alanylation (DLT) pathway modifies bacterial cell walls, impacting antibiotic resistance. This study reveals DltD

Keywords:

DLT pathway DltB MBOAT Staphylococcus aureus (S. aureus)acyltransferase cell wall membrane protein pathway reconstitution teichoic acid

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In vitro Reconstitution of the Active T. castaneum Telomerase

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Published on: July 14, 2011

Area of Science:

Microbiology
Bacterial Cell Wall Biology
Antibiotic Resistance Mechanisms

Background:

Gram-positive bacterial cell wall modifications are crucial for antibiotic resistance and pathogenesis.
The d-alanylation (DLT) pathway, a key modification, is not fully understood.
The DLT pathway involves membrane proteins DltB and DltD with unclear functions in d-alanine transfer.

Purpose of the Study:

To investigate the role of DltD in the d-alanylation of lipoteichoic acid (LTA) in *Staphylococcus aureus*.
To elucidate the mechanism of d-alanine transfer within the DLT pathway.
To develop assays for studying the bacterial DLT pathway.

Main Methods:

Utilized synthetic lethal interactions to confirm gene essentiality in the DLT pathway.
Employed radiolabeled d-alanine to detect d-alanyl-LTA in cells and vesicles.
Developed a partial pathway reconstitution system using cell-derived vesicles and purified proteins.
Analyzed DltD mutants to identify essential residues for d-alanylation activity.

Main Results:

Confirmed the essentiality of DLT pathway genes for LTA d-alanylation in *S. aureus*.
Demonstrated that DltB vesicles require DltA, DltC, and DltD for LTA d-alanylation, independent of LtaS.
Identified Ser-70 and His-361 in DltD as critical for catalytic activity.
Proposed a catalytic dyad mechanism for DltD in d-alanine transfer.

Conclusions:

Developed novel assays for investigating the bacterial DLT pathway.
Uncovered a direct role for DltD in the d-alanylation of LTA.
Proposed a catalytic mechanism for DltD involving a dyad, advancing understanding of this essential bacterial process.