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 IV mutation literature information.


  A nontoxic mutant of cholera toxin elicits Th2-type responses for enhanced mucosal immunity.
 PMID: 9144226       1997       Proc Natl Acad Sci U S A
Abstract: Both S61F and native CT enhanced the induction of ovalbumin-specific CD4(+) T cells in lung and splenic tissues, and these T cells produced a Th2-type cytokine pattern of interleukin 4 (IL-4), IL-5, IL-6, and IL-10 as determined by analysis of secreted proteins and by quantitation of cytokine-specific mRNA.
Abstract: Further, high protein-specific IgA antibody responses were observed in nasal and vaginal washes, saliva, and fecal extracts as well as increased numbers of IgG and IgA antibody forming cells in cervical lymph nodes and lung tissues of mice intranasally immunized with these proteins and S61F or native CT, but not with recombinant CT-B or protein alone.
Abstract: Mice immunized with these proteins plus S61F showed high serum titers of protein-specific IgG and IgA antibodies that were comparable to those induced by native CT.
Abstract: Mice were intranasa


  The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR.
 PMID: 9150402       1997       Journal of molecular biology
Abstract: Through site-directed mutagenesis, eight cysteine (Cys) mutants in the fusion peptide region of HA2 (A5C, I6C, A7C, G8C, I10C, N12C, G13C, W14C) were generated and modified with a nitroxide spin label.


  A single sequence change destabilizes the influenza virus neuraminidase tetramer.
 PMID: 9299618       1997       Virology
Abstract: A single change (E119G) in the influenza A virus N9 neuraminidase (NA) results in resistance of the enzyme to the NA inhibitor 4-Guanidino-Neu5Ac2en (4-GuDANA).
Abstract: It is suggested that the E119G alteration in the 4-GuDANA-resistant NA leads to the abrogation of this interaction and thus to the instability of the NA tetramers.
Abstract: These small crystals were of sufficient quality to yield X-ray crystallographic data which confirmed the E119G change and demonstrated the presence of electron density representing either a strong structural-water molecule or an anionic species in place of the glutamate carboxylate.


  Tyrosine-dependent basolateral sorting signals are distinct from tyrosine-dependent internalization signals.
 PMID: 9334200       1997       The Journal of biological chemistry
Abstract: Converting cysteine 543 to tyrosine in the influenza virus hemagglutinin (HA) introduces both a basolateral sorting signal and an internalization signal into the HA cytoplasmic domain.
Abstract: For HA C543Y, the same sequence positions were important for both basolateral sorting and internalization, but the two functions responded differently to individual amino acid replacements, indicating that they were distinct.
Abstract: To test this hypothesis, second-site mutations were introduced into HA C543Y or HA+8 to determine if the internalization and basolateral sorting functions can be separated.


  The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication.
 PMID: 8551626       1996       Journal of virology
Abstract: A NOTAIL virus containing an additional mutation (Ser-12 to Pro) in the transmembrane domain incorporated three times more NA molecules into virions than did the NOTAIL parent but approximately half of the amount incorporated by the wild-type virus.


  Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells.
 PMID: 8609159       1996       The Journal of cell biology
Abstract: In addition, we also have studied the transport of a hemagglutinin mutant (Cys543Tyr) which is basolateral in MDCK cells.


  On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin.
 PMID: 8611525       1996       Biochemistry
Abstract: Extensive intramolecular cysteine-cysteine cross-linking was observed not only for F63C and I66C but also for H64C.
Abstract: Four consecutive single-cysteine mutants, F63C, H64C, Q65C, and I66C, were generated using site-directed mutagenesis.


  Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en.
 PMID: 8627706       1996       Journal of virology
Abstract: Sequence analysis established that a substitution had occurred in the NA (Arg-249 to Lys) and in the HA2 subunit of the hemagglutinin (Gly-75 to Glu), in the vicinity of the proposed second sialic acid binding site.


  Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4-amino-Neu5Ac2en and 4-guanidino-Neu5Ac2en.
 PMID: 8787876       1996       Antimicrobial agents and chemotherapy
Abstract: NWS/G70C virus (H1N9) was cultured in each drug by limiting-dilution passaging.


  Neurovirulence of influenza A virus.
 PMID: 8799206       1996       Journal of neurovirology
Abstract: In the M gene, two specific amino acid substitutions in the M1 protein have been observed, Ala41-->Val and Thr139-->Ala, which correlate with increased virulence for mouse.



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