polybasic


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polybasic

 [pol″e-ba´sik]
having several replaceable hydrogen atoms.

pol·y·ba·sic

(pol'ē-bā'sik),
Having more than one replaceable hydrogen atom, denoting an acid with a basicity greater than 1.

polybasic

/poly·ba·sic/ (-ba´sik) having several replaceable hydrogen atoms.

pol·y·ba·sic

(pol'ē-bā'sik)
Having more than one replaceable hydrogen atom; denoting an acid with a basicity greater than 1.

polybasic

having several replaceable hydrogen atoms.
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References in periodicals archive ?
Compound 48/80 and other polybasic compounds are shown to activate G proteins (20,21).
This evidence suggests that the polybasic HA cleavage site was acquired progressively through multiple mutations within the avian species in a subclade of the A(H7N9) viruses.
The polybasic hemagglutinin (HA) cleavage site sequence RNSPLRERRRKR*GLF indicated a highly pathogenic phenotype.
The HA cleavage site showed polybasic properties RNSPLRERRRKR*GLFGAIA, confirming the high pathogenicity of the virus.
This process showed the polybasic cleavage site PLRERRRKR/ GLF from multiple bird swab and tissue samples from each shed.
The amino acid sequence of the HA1/HA2-connecting peptide of HA is a major determinant of pathogenicity in terrestrial poultry, and the pathogenicity of highly pathogenic subtype H5N1 and H7N3 viruses is influenced by the presence of a polybasic cleavage site in the connecting peptide (32).
The virus's hemagglutinin (HA) cleavage site had the polybasic amino acid sequence PQRERRRKRGLF, which is characteristic of HPAIVs (22).
9 * PB, polybasic protein; 008, A/duck/eastern China/008/2008(H5N5); 108, A/duck/eastern China/108/2008(H5N1); 031, A/duck/eastern China/031/2009(H5N5); 909, A/duck/eastern China/909/2009(H5N1); 013, A/duck/Yangzhou/013/2008(H6N5); PA, polymerase acidic protein; HA, hemagglutinin; NP, nucelocapsid protein; NA, neuraminidase; M, matrix protein; NS, nonstructural protein.
The respiratory tract of poultry and gastrointestinal tract of waterfowl are replication sites for AIVs, and poultry are incubators for the progression of low-pathogenicity avian influenza (LPAI) virus into highly pathogenic avian influenza (HPAI) virus (4-6), usually through the acquisition of polybasic amino acids at the HA cleavage site.
We found that the H cleavage site of the selected influenza subtype H5N1 isolates (determined from the Veterinary Laboratory Agency) contained polybasic amino acids, which are characteristic of HPAI A viruses (Table 2).
Because highly pathogenic influenza (H5N1) subtypes may kill embryonated eggs, use of viruses that are no longer pathogenic, such as H5 (which lacks the polybasic cleavage site), to reduce the virulence of influenza (H5N1) vaccine strains so that these can be efficiently propagated in eggs for vaccine production is feasible (10).