BIOMAT Database Logo BIOMAT Database Logo

Capsular sialic acid prevents activation of the alternative complement pathway by type III, group B streptococci. 1982

M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller

UI MeSH Term Description Entries
D007231 Infant, Newborn An infant during the first 28 days after birth. Neonate,Newborns,Infants, Newborn,Neonates,Newborn,Newborn Infant,Newborn Infants
D009439 Neuraminidase An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992) Sialidase,Exo-alpha-Sialidase,N-Acylneuraminate Glycohydrolases,Oligosaccharide Sialidase,Exo alpha Sialidase,Glycohydrolases, N-Acylneuraminate,N Acylneuraminate Glycohydrolases,Sialidase, Oligosaccharide
D011135 Polysaccharides, Bacterial Polysaccharides found in bacteria and in capsules thereof. Bacterial Polysaccharides
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D003167 Complement Activation The sequential activation of serum COMPLEMENT PROTEINS to create the COMPLEMENT MEMBRANE ATTACK COMPLEX. Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES. Activation, Complement,Activations, Complement,Complement Activations
D003170 Complement Pathway, Alternative Complement activation initiated by the interaction of microbial ANTIGENS with COMPLEMENT C3B. When COMPLEMENT FACTOR B binds to the membrane-bound C3b, COMPLEMENT FACTOR D cleaves it to form alternative C3 CONVERTASE (C3BBB) which, stabilized by COMPLEMENT FACTOR P, is able to cleave multiple COMPLEMENT C3 to form alternative C5 CONVERTASE (C3BBB3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX. Alternative Complement Pathway,Properdin Pathway,Alternative Complement Activation Pathway,Complement Activation Pathway, Alternative
D003175 Complement C2 A component of the CLASSICAL COMPLEMENT PATHWAY. C2 is cleaved by activated COMPLEMENT C1S into COMPLEMENT C2B and COMPLEMENT C2A. C2a, the COOH-terminal fragment containing a SERINE PROTEASE, combines with COMPLEMENT C4B to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE). C2 Complement,Complement 2,Complement Component 2,C2, Complement,Complement, C2,Component 2, Complement
D003176 Complement C3 A glycoprotein that is central in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C3 can be cleaved into COMPLEMENT C3A and COMPLEMENT C3B, spontaneously at low level or by C3 CONVERTASE at high level. The smaller fragment C3a is an ANAPHYLATOXIN and mediator of local inflammatory process. The larger fragment C3b binds with C3 convertase to form C5 convertase. C3 Complement,C3 Precursor,Complement 3,Complement C3 Precursor,Complement Component 3,Precursor-Complement 3,Pro-C3,Pro-Complement 3,C3 Precursor, Complement,C3, Complement,Complement, C3,Component 3, Complement,Precursor Complement 3,Precursor, C3,Precursor, Complement C3,Pro C3,Pro Complement 3
D003179 Complement C3b The larger fragment generated from the cleavage of COMPLEMENT C3 by C3 CONVERTASE. It is a constituent of the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb), and COMPLEMENT C5 CONVERTASES in both the classical (C4b2a3b) and the alternative (C3bBb3b) pathway. C3b participates in IMMUNE ADHERENCE REACTION and enhances PHAGOCYTOSIS. It can be inactivated (iC3b) or cleaved by various proteases to yield fragments such as COMPLEMENT C3C; COMPLEMENT C3D; C3e; C3f; and C3g. C3b Complement,C3bi,Complement 3b,Complement Component 3b,Inactivated C3b,iC3b,C3b, Complement,C3b, Inactivated,Complement, C3b,Component 3b, Complement
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Capsular sialic acid limits C5a production on type III group B streptococci.
April 1999, Infection and immunity,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation.
January 1987, Infection and immunity,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Capsular polysaccharide regulates neutrophil complement receptor interactions with type III group B streptococci.
July 1993, Infection and immunity,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Growth of group B streptococci in human serum leads to increased cell surface sialic acid and decreased activation of the alternative complement pathway.
February 1994, Canadian journal of microbiology,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Type-specific antibody prevents platelet aggregation induced by group B streptococci type III.
April 1986, The Journal of laboratory and clinical medicine,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Activation of the alternative complement pathway by Haemophilus influenzae type B.
April 1977, Infection and immunity,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Activation of the alternative complement pathway by enveloped viruses containing limited amounts of sialic acid.
October 1981, Virology,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Group B streptococci invade endothelial cells: type III capsular polysaccharide attenuates invasion.
February 1993, Infection and immunity,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Opsonophagocytosis of group B streptococci: the role of sialic acid.
January 1985, Journal of clinical pathology,
M S Edwards, and D L Kasper, and H J Jennings, and C J Baker, and A Nicholson-Weller
Structural elucidation of type III group B Streptococcus capsular polysaccharide using molecular dynamics simulations: the role of sialic acid.
April 2005, Carbohydrate research,
Copied contents to your clipboard!