An Unusual Carbohydrate Conformation is Evident in Moraxella catarrhalis Oligosaccharides
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چکیده
منابع مشابه
An Unusual Carbohydrate Conformation is Evident in Moraxella catarrhalis Oligosaccharides.
Oligosaccharide structures derived from the lipooligosaccharide of M. catarrhalis show that the highly branched glucose-rich inner core of the oligosaccharide has an altered conformation compared to the most truncated tetra-glucose-Kdo lgt1/4Δ oligosaccharide structure. Addition of one residue each to the (1-4) and (1-6) chains to give the lgt2Δ oligosaccharide is the minimum requirement for th...
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The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly conserved among M. catarrhalis strains and which encoded a predicted protein with significant homology to the Hfq protein of Escherichia coli. This ...
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Moraxella catarrhalis O35E was shown to synthesize a 105-kDa protein that has similarity to both acid phosphatases and autotransporters. The N-terminal portion of the M. catarrhalis acid phosphatase A (MapA) was most similar (the BLAST probability score was 10(-10)) to bacterial class A nonspecific acid phosphatases. The central region of the MapA protein had similarity to passenger domains of ...
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BACKGROUND Peritonitis continues to be a major complication of peritonitis in peritoneal dialysis patients. Recent advances in connectology and better patient training have decreased the incidence of peritonitis in the last two decades. Peritonitis in PD patients is usually due to gram positive and less often due to gram negative organisms. Herein we report a case of peritonitis due to Moraxell...
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Original Article Moraxella catarrhalis lower respiratory tract infection Beta Lactamase and Pneumonia
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ژورنال
عنوان ژورنال: Molecules
سال: 2015
ISSN: 1420-3049
DOI: 10.3390/molecules200814234