J. M. Atack

Actinobacillus pleuropneumoniae encodes multiple phase-variable DNA methyltransferases that comprise distinct phasevarions

This study identifies multiple phase-variable DNA methyltransferases in Actinobacillus pleuropneumoniae, showing their role in regulating phasevarions and pathogenic traits.

ModA phasevarions regulate adherence of non-typeable Haemophilus influenzae to the host airway in a tissue-specific manner

This study investigates how ModA phasevarions regulate NTHi adherence to different host airway substrates, identifying specific adhesins involved in tissue-specific interactions.

A phasevarion controls multiple virulence traits, including expression of vaccine candidates, in Streptococcus pneumoniae

This study shows that the SpnIII phasevarion in S. pneumoniae affects multiple virulence traits and vaccine candidate expression, highlighting its importance in vaccine design.

Characterisation of the phase-variable autotransporter Lav reveals a role in host cell adherence and biofilm formation in Non-Typeable Haemophilus influenzae

This study characterizes the phase-variable autotransporter Lav in NTHi, showing its role in host cell adherence and biofilm formation.

Streptococcus suis encodes multiple allelic variants of a phase-variable Type III DNA methyltransferase, ModS, that control distinct phasevarions

This paper identifies multiple allelic variants of the phase-variable Type III DNA methyltransferase ModS in Streptococcus suis, showing they regulate distinct phasevarions affecting growth and antibiotic resistance.

Systematic analysis of REBASE identifies numerous Type I restriction-modification systems that contain duplicated, variable hsdS specificity genes that randomly switch methyltransferase specificity by recombination.

The paper identifies 5.9% of Type I R-M systems with duplicated hsdS genes that enable phase-variation through recombination, found in pathogens like Enterococcus faecalis and Listeria monocytogenes.

The non-typeable Haemophilus influenzae major adhesin Hia is a dual function lectin that binds to human-specific respiratory tract sialic acid glycan receptors.

This paper identifies Hia, a major adhesin in NTHi, as a dual-function lectin that binds to human-specific sialic acid glycans, mimicking the combined activity of HMW1 and HMW2 adhesins.