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Amelie83 Views: 141
Published: 4 years ago

Cable Bacteria?

Cable bacteria?

Anyone have anymore information on this or thoughts on this possibly relating to Morgellons?

Organosulfur compound metabolism in the human pathogen
Haemophilus influenzae
Dk Seti Maimonah Othman1, Noor Marian Muda1, Rabeb Dhouib1, Horst J Schirra1, 2,
Alastair G McEwan1, Ulrike Kappler1
1 School of Chemistry and Molecular Biosciences, The University of Queensland, Australia
2 Centre for Advanced Imaging, The University of Queensland, Australia
Non-typeable Haemophilus influenzae (NTHi) is a host-adapted pathogen that causes a
variety of acute and chronic infections including otitis media, non-CF bronchiectasis and
chronic obstructive pulmonary disease (COPD). NtHi generates energy via a ‘respiration
assisted fermentation’ that relies on a mixed acid type fermentation linked to a versatile
respiratory chain used for redox balancing. This respiratory chain contains two putative
sulfoxide converting molybdenum enzymes, a DmsA-type dimethylsulfoxide (DMSO)
reductase and a TorZ-like enzyme. Both enzymes were highly expressed under mostly
anaerobic conditions, which is in keeping with established roles and expression patterns
for such enzymes in e.g. E. coli. However, the main substrates for either of these
enzymes, DMSO and trimethylaminoxide (TMAO), are largely absent from the human
body, calling into question the physiological significance of these enzymes is in H.
Our data show that both enzymes are conserved in Pasteurellaceae, and form separate
clades within their respective enzyme families, indicating important roles in pathogen
physiology. In order to elucidate the properties and physiological roles of these
enzymes, we have created and studied dmsA & torZ mutant strains of H. influenzae. The
ΔdmsA strain showed defects in biofilm formation and colonization of epithelial cells,
while the ΔtorZ strain showed minor changes in tissue cell colonization. Our
characterization of the purified TorZ enzyme showed low affinities to DMSO and TMAO,
but high affinity for methionine sulfoxide as a substrate, further corroborating the fact
that this group of enzymes fulfils a novel function in bacterial physiology. Gene
expression patterns varied for the two sulfoxide reductases varied in different strains of
H. influenzae, which may be indicative of niche specific adaptation. Based on our results
we propose that DmsA & TorZ may act on sulfoxides produced from e.g. sulfur
containing amino acids during interaction of NTHi with the immune system.

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