IV mutation literature information.


  Generation and characterization of a mutant of influenza A virus selected with the neuraminidase inhibitor BCX-140.
 PMID: 9559786       1998       Antimicrobial agents and chemotherapy
Abstract: One is a change in HA1 of Ala-133 to Thr, a residue close to the binding site, while the other change was Arg-132 of HA1 to Gln, which in HA1 of serotype H3 is a sialic acid contact (Asn-137).


  Postreassortment changes in influenza A virus hemagglutinin restoring HA-NA functional match.
 PMID: 9601502       1998       Virology
Abstract: One substitution, N248D in HA1, is the same in two independently selected nonaggregating variants.


  Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase.
 PMID: 9655825       1998       Structure (London, England
Abstract: CONCLUSIONS: The Arg292-->Lys variant of influenza neuraminidase affects the binding of substrate by modification of the interaction with the substrate carboxylate.
Abstract: Inhibitors that have replacements for the glycerol at position 6 are further affected in the Arg292-->Lys variant because of structural changes in the binding site that apparently raise the energy barrier for the conformational change in the enzyme required to accommodate such inhibitors.
Abstract: RESULTS: The neuraminidase variant Arg292-->Lys is modified in one of three arginine residues that encircle the carboxylate group of the substrate.


  The interaction of neuraminidase and hemagglutinin mutations in influenza virus in resistance to 4-guanidino-Neu5Ac2en.
 PMID: 9656997       1998       Virology
Abstract: This variant has been found to also harbor a hemagglutinin (HA) mutation in the receptor binding site, Ser 186 to Phe.
Abstract: We have previously described a 4-guanidino-Neu5Ac2en (zanamivir)-resistant neuraminidase (NA) variant G70C4-G, with an active site mutation Glu 119 to Gly.


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 9683567       1998       Virology
Abstract: This variant, which has a mutation in the active site, Glu 119 Gly (E119G), has the same specific activity as the wild-type neuraminidase (NA), but is inherently unstable, as measured by loss of both enzyme activity and NC10 monoclonal antibody reactivity.


  Critical interactions in binding antibody NC41 to influenza N9 neuraminidase: amino acid contacts on the antibody heavy chain.
 PMID: 9692956       1998       Biochemistry
Abstract: Asp97 forms a salt link with NA critical contact Lys434; of the four mutants, D97K shows the largest reduction in binding to NA.
Abstract: Association constants (Ka) for wild-type and mutant scFvs are as follows: wild type, 2 x 10(7) M-1; Asn31-->Gln, 2 x 10(7) M-1; Glu96-->Asp, 1 x 10(7) M-1; Asp97-->Lys, 6 x 10(6) M-1; and Asn98-->Gln, 8 x 10(6) M-1.
Abstract: Mutant N98Q also shows reduced binding, most likely through the loss of interaction with NA residue Thr401.
Abstract: NC41 residue Glu96 interacts with NA critical contact Ser368, yet E96D showed only a 2-fold reduction in bindi


  The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction.
 PMID: 9696865       1998       Journal of virology
Abstract: Our results showed that the Ser-to-Gly mutation at position 228, in addition to the Leu-to-Gln mutation at position 226 of the HA of the H3 subtype, is critical for human virus HA to support virus replication in duck intestine.


  Efficient induction of cytotoxic CD8+ T cells against exogenous proteins: establishment and characterization of a T cell line specific for the membrane protein ActA of Listeria monocytogenes.
 PMID: 9754551       1998       European journal of immunology
Abstract: To overcome the potential problem of presentation of the immunodominant epitope LL091-99 by H-2Kd, a variant LLO92A was established in which Tyr 92 was replaced by Ala.


  Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus.
 PMID: 9780244       1998       The Journal of infectious diseases
Abstract: A hemagglutinin mutation (198 Thr-->Ile) reduced the virus affinity for receptors found on susceptible human cells.
Abstract: A mutation in the neuraminidase active site (152 Arg-->Lys) led to a 1000-fold reduction in the enzyme sensitivity to zanamivir.


  Mucosal immunoadjuvant activity of recombinant Escherichia coli heat-labile enterotoxin and its B subunit: induction of systemic IgG and secretory IgA responses in mice by intranasal immunization with influenza virus surface antigen.
 PMID: 9796066       1998       Vaccine
Abstract: However, supplementation of the antigen with E112K or rLTB resulted in a substantial stimulation of the serum IgG level and in induction of a strong S-IgA response in the nasal cavity.
Abstract: Mice were immunized intranasally (i.n.) with influenza virus subunit antigen, consisting mostly of the isolated surface glycoprotein hemagglutinin (HA), supplemented with either recombinant LTB (rLTB), a nontoxic LT mutant (E112K, with a Glu112-->Lys substitution in the A subunit), or LT holotoxin, and the induction of systemic IgG and local S-IgA responses was evaluated by direct enzyme-linked immunosorbent assay (ELISA).
Abstract: The adjuvant activity of E112K or rLTB under these conditions was essentially the same as that of the LT holotoxin.



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