Neuraminidase expressed by Streptococcus pneumoniae desialylates the lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzae: a paradigm for interbacterial competition among pathogens of the human respiratory tract.
about
The role of innate immune responses in the outcome of interspecies competition for colonization of mucosal surfacesDiversity of microbial sialic acid metabolismThe Ashwell receptor mitigates the lethal coagulopathy of sepsisThe role of respiratory viruses in the etiology of bacterial pneumonia: An ecological perspectiveNasopharyngeal Bacterial Carriage in the Conjugate Vaccine Era with a Focus on PneumococciPneumococcal carbohydrate transport: food for thoughtCo-infection subverts mucosal immunity in the upper respiratory tractStructural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidaseSialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporterExposure of Thomsen-Friedenreich antigen in Streptococcus pneumoniae infection is dependent on pneumococcal neuraminidase A.Sialic acid, periodontal pathogens and Tannerella forsythia: stick around and enjoy the feast!Nontypeable Haemophilus influenzae inhibits autolysis and fratricide of Streptococcus pneumoniae in vitroInfluenza promotes pneumococcal growth during coinfection by providing host sialylated substrates as a nutrient source.Activation of brain endothelium by pneumococcal neuraminidase NanA promotes bacterial internalization.Density interactions among Streptococcus pneumoniae, Haemophilus influenzae and Staphylococcus aureus in the nasopharynx of young Peruvian children.Composition and immunological significance of the upper respiratory tract microbiota.Viral and bacterial interactions in the upper respiratory tractVariation in the presence of neuraminidase genes among Streptococcus pneumoniae isolates with identical sequence types.Sialic acid transport contributes to pneumococcal colonization.Bacterial neuraminidase facilitates mucosal infection by participating in biofilm productionHyaluronic acid derived from other streptococci supports Streptococcus pneumoniae in vitro biofilm formation.Genome analysis of Flaviramulus ichthyoenteri Th78(T) in the family Flavobacteriaceae: insights into its quorum quenching property and potential roles in fish intestineSerum antibodies to pneumococcal neuraminidase NanA in relation to pneumococcal carriage and acute otitis mediaProcession to pediatric bacteremia and sepsis: covert operations and failures in diplomacyLeukocyte inflammatory responses provoked by pneumococcal sialidase.Role of complement in defense of the middle ear revealed by restoring the virulence of nontypeable Haemophilus influenzae siaB mutants.Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factorStreptococcus pneumoniae can utilize multiple sources of hyaluronic acid for growth.Desialylation of Neisseria gonorrhoeae Lipooligosaccharide by Cervicovaginal Microbiome Sialidases: The Potential for Enhancing Infectivity in Men.Impact of micro-environmental changes on respiratory tract infections with intracellular bacteria.Nasopharyngeal bacterial interactions in children.Microbial interactions during upper respiratory tract infectionsVirulence factors in pneumococcal respiratory pathogenesis.What makes pathogens pathogenic.The surface-anchored NanA protein promotes pneumococcal brain endothelial cell invasion.Role of Streptococcus pneumoniae Proteins in Evasion of Complement-Mediated Immunity.Innate immune recognition and inflammation in Neisseria meningitidis infection.Sialic acid-mediated gene expression in Streptococcus pneumoniae and role of NanR as a transcriptional activator of the nan gene cluster.Pneumococcal neuraminidase activates TGF-β signalling.Three surface exoglycosidases from Streptococcus pneumoniae, NanA, BgaA, and StrH, promote resistance to opsonophagocytic killing by human neutrophils.
P2860
Q21131627-EA508F36-A1E5-410D-A56A-D06FBDFA6D25Q24594315-FFE184F5-2784-432A-8519-F667D595647CQ24596452-27F30FFB-6CD6-48D6-9A93-D1CD2F20164BQ26765407-655D18AA-457B-46DD-B89E-CCCE714A5007Q26782298-8CD05C4B-F054-478B-A1CD-32342BF54224Q26830554-0947BE3A-E532-419D-9358-954C04077454Q27002952-DDE8EFA5-026A-4F36-B6FE-79CDD2924DE8Q27652026-B5CFA92E-D08D-4FB9-8815-31AF8B527E95Q28279859-47A515C7-F6FE-406A-9B99-BFF9EC4A42B7Q33394397-E96A7CA4-9E70-4BCC-86DC-8280C739A262Q33727227-44078ED1-4C9D-4C2C-A8D5-AE4133537520Q33840679-354A10CF-5750-4B6C-AB3D-C3CE902CBDD4Q33896536-244EB990-B1FC-422D-A661-9CAC76565A82Q34146012-9C2904D7-5D33-4E64-9D41-88C17BF13BB2Q34398550-6A0B9696-59C0-4436-8AEB-B792036D7090Q34542383-C924A732-159D-4C0F-9946-3D333D9453BBQ34550727-7063064B-FC9C-46D0-B5E5-CF4BCE4772D7Q34681065-3FFAEB1C-0D99-4933-A053-FF4E8B692345Q34739576-1DE21F39-DA9D-4853-8E8A-A73C57C18145Q34803233-23B2C007-75FC-4D7E-ADB2-27D416A27930Q35028623-973E569E-100D-4931-83E4-69ADA6D34FE5Q35071566-3533FFC3-2944-4FAB-A86D-BA4A1EB7D44FQ35075156-10AF0AB7-EB78-4CF4-8486-05CADED09570Q35125036-3B836DD7-7002-4114-B509-47981FDF6EA2Q35652328-0967CC67-1BF7-48B3-9BD8-13379144A8A2Q35689035-B20CAD6C-0D43-425B-AE94-9B31BF13852EQ35750685-44431E53-9751-48D6-ADB7-212BA112CB11Q35867630-5C8F879C-5AB4-45BF-A7C1-97D7768E5113Q36089294-082D5822-B2E0-4A73-AA6F-413FBE7074D8Q36100313-F8F6039F-BA63-4337-8A21-BAA29EC393D8Q36574329-94DAFBA3-A796-4AF7-8F76-DA6E08B6E627Q37028479-EE15BE27-E67D-49C4-B801-24B9B83AB4AEQ37119044-4F195EC2-5DC0-4986-82D7-D9F2C2ED4E84Q37206311-7AB23F01-702A-4B8E-AE82-2E9EA1A6FB77Q37331532-710207D9-46A8-42C0-9D86-8EBE3C332104Q39164566-6C921D59-520D-4D73-B0AC-5642100B75F1Q39196108-5CC9CBA3-CCC9-49D7-987C-651F507562B6Q39518202-934644B8-F8F0-49B6-8F6A-0E2F781CD86BQ40117406-F8AD5CA4-86A2-44A3-BF9B-250DAF24EA74Q40330903-08C41E96-5FA2-4A2A-9FF2-73D56A49C865
P2860
Neuraminidase expressed by Streptococcus pneumoniae desialylates the lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzae: a paradigm for interbacterial competition among pathogens of the human respiratory tract.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Neuraminidase expressed by Str ...... f the human respiratory tract.
@en
Neuraminidase expressed by Str ...... f the human respiratory tract.
@nl
type
label
Neuraminidase expressed by Str ...... f the human respiratory tract.
@en
Neuraminidase expressed by Str ...... f the human respiratory tract.
@nl
prefLabel
Neuraminidase expressed by Str ...... f the human respiratory tract.
@en
Neuraminidase expressed by Str ...... f the human respiratory tract.
@nl
P2860
P1476
Neuraminidase expressed by Str ...... f the human respiratory tract.
@en
P2093
Elizabeth A Shakhnovich
Samantha J King
P2860
P304
P356
10.1128/IAI.70.12.7161-7164.2002
P407
P577
2002-12-01T00:00:00Z