Deacetylation of sialic acid by esterases potentiates pneumococcal neuraminidase activity for mucin utilization, colonization and virulence

PLoS Pathogens

Volumn 13, Issue 3, 2017, Pages

  Kahya, Hasan F ^a,b   Andrew, Peter W ^a   Yesilkaya, Hasan ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b UNIVERSITY OF MOSUL   (Iraq)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; COMPLEMENTARY DNA; ESTERASE; LACTATE DEHYDROGENASE; MUCIN; RECOMBINANT PROTEIN; SERINE; SIALIC ACID; SIALIDASE; TRIBUTYRIN; N ACETYLNEURAMINIC ACID;

ARTICLE; CARBON SOURCE; DEACETYLATION; DISEASE COURSE; DRUG POTENTIATION; ENZYME KINETIC ASSAY; GENE EXPRESSION REGULATION; HUMAN; LUNG PARENCHYMA; MICROBIAL COLONIZATION; MOLECULAR CLONING; NASOPHARYNX; NONHUMAN; POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; STREPTOCOCCUS PNEUMONIA; SURVIVAL TIME; VIRULENCE; ACETYLATION; ANIMAL; DISEASE MODEL; FEMALE; METABOLISM; MOUSE; PATHOGENICITY; PHYSIOLOGY; REAL TIME POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS PNEUMONIAE;

ACETYLATION; ANIMALS; DISEASE MODELS, ANIMAL; ESTERASES; FEMALE; MICE; MUCINS; MUTAGENESIS, SITE-DIRECTED; N-ACETYLNEURAMINIC ACID; NEURAMINIDASE; PNEUMONIA, PNEUMOCOCCAL; REAL-TIME POLYMERASE CHAIN REACTION; STREPTOCOCCUS PNEUMONIAE; VIRULENCE;

EID: 85016491894     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1006263     Document Type: Article

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