See Also: batroxostatin(medicine)
Herbal medicine (botanical medicine, herbology, phytomedicine)(health)
Medicine Lodge Memorial Hospital- Medicine Lodge(health)
influenza B(medicine)
influenza(encyclopedia)
influenza(dictionary)
Influenza(medicine)
Influenza(health)
Influenza c(medicine)
Influenza a(medicine)

Influenza virus (medicine) and batroxostatin (medicine)


Influenza virus (medicine)


influenza virus
<organism, virology> Member of the Orthomyxoviridae that causes influenza in humans. There are three types of influenza virus.

Each type of virus has a stable nucleoprotein group antigen common to all strains of the type, but distinct from that of the Other type; each also has a mosaic of surface antigens (haemagglutinin and neuraminidase) which characterise the strains and which are subject to variations of two kinds: 1) a rather continual drift that occurs independently within the haemagglutinin and neuraminidase antigens; 2) after a period of years, a sudden shift (notably in type A virus of human origin) to a different haemagglutinin or neuraminidase antigen. The sudden major shifts are the basis of subdivisions of type A virus of human origin.

Type A causes the world wide epidemics (pandemics) of influenza and can infect Other mammals and birds.

Type B only affects humans.

Type C causes only a mild infection.

Types A and B virus evolve continuously, resulting in changes in the antigenicity of their spike proteins, preventing the development of prolonged immunity to infection. The spike proteins, external haemagglutinin and neuraminidase have been studied as models of membrane glycoproteins.

Strain notations indicate type, geographic origin, year of isolation, and, in the case of type A strains, the characterizing subtypes of haemagglutinin and neuraminidase antigens (e.g., A/Hong Kong/1/68 (H3 N2); B/Hong Kong/5/72).


batroxostatin (medicine)


batroxostatin -->
disintegrin
<protein> Peptides found in the venoms of various snakes of the viper family, that inhibit the function of some integrins of the _1 and _3 classes. They were first identified as inhibitors of platelet aggregation and were subsequently shown to bind with high affinity to integrins and to block the interaction of integrins with RGD containing proteins for example they block the binding of the platelet integrin _IIb_3 to fibrinogen. Disintegrins are effective inhibitors at molar concentrations 500-2000x lower than short RGDX peptides. They are cysteine rich peptides ranging from 45 to 84 amino acids in length and almost all of them have a conserved RGD sequence on a _ turn, presumed to be the site that binds to integrins. The assumption is that their biological role in the venom is to inhibit blood clotting. Found in many snake species, where they are called variously albolabrin, applagin, batroxostatin, bitistatin, echistatin, elegantin, flavouridin, halysin, kistrin, triflavin and trigramin.