a environment maryland 261 2006 h7n3  (ATCC)

Journal: Saudi Journal of Biological Sciences

Article Title: Live attenuated influenza vaccine induces broadly cross-reactive mucosal antibody responses to different influenza strains in tonsils

doi: 10.1016/j.sjbs.2023.103809

Figure Lengend Snippet: LAIV did not induce anti-H7N3 HA IgG antibody production. No significant level of specific anti-HA IgG antibody to H7N3 was detected compared with unstimulated cells (n = 15, p > 0.05). Means and standard errors are shown.

Article Snippet: Purified recombinant HA proteins of pH1N1 (A/California/04/2009,VR-1894DQ),sH1N1 (A/Brisbane/59/2007, VR-1742), sH3N2 (A/Brisbane/10/2007, VR-1881), aH5N1 (A/Vietnam/1203/2004, VR-1931), A/Hong Kong/8/68, VR-1679), and H7N3 (A/Canada/RV444/04, VR-1641) were from Biodefense and Emerging Infections Research Resources Repository (BEI resources ATCC (Manassas VA, USA).

Techniques:

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Comparison of the HAs of A/Equine/New York/43/73 H7N7 and A/Turkey/Italy/214845/02 H7N3. (A) RBS structure of H7eq (yellow) in complex with 3′-GcLN (NeuGcα2-3Galβ1-4GlcNAc; cyan), deposited in the Protein Data Bank (PDB) under accession code 7T1V . (B) Electron density 2Fo-Fc map at 1σ level for receptor analog 3′-GcLN. (C) RBS structure of H7tu (gray) in complex with 3′-SLN (NeuAcα2-3Galβ1-4GlcNAc; green) (PDB code 4BSI ). (D) Superimposition of the RBS structures of H7eq and H7tu and their ligands 3′-GcLN and 3′-SLN. The coloring scheme follows that of panels A and C. (E) Alignment of the RBS residues of H7eq and H7tu, with amino acid positions (H3 numbering) indicated above the alignment, nonconserved residues highlighted in black, and dots indicating identical amino acids. A full alignment of the HAs is shown in Fig. S1.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Comparison

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Evaluation of the binding specificities of single mutants of the HA of A/Turkey/Italy/214845/02 H7N3. (A) Synthetic glycans printed on the microarray ( n = 6), either without sialic acid (structures 1 to 3; light gray), with α2,6-linked NeuAc (structures 4 to 6; black), α2,3-linked NeuAc (structures 7 to 9; dark gray), α2,6-linked NeuGc (structures 10 to 12; red), or α2,3-linked NeuGc (structures 13 to 15; blue). Structures 1, 4, 7, 10, and 13 contain one LacNAc repeat, structures 2, 5, 8, 11, and 14 have two repeats, and structures 3, 6, 9, 12, and 15 contain three repeats . The glycan microarray, which is representative of two independent assays, was used to determine the receptor specificity of recombinantly expressed HA of the H7tu wild type (WT) (B) and S128T (C), I130V (D), A135E (E), G144R (F), A159G+A160V (G), T189A (H), K193R (I), and A219P (J) mutants.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Microarray, Glycoproteomics

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Evaluation of the binding specificities of double and triple mutants of the HA of A/Turkey/Italy/214845/02 H7N3. The glycan microarray as described in the legend to was used, containing glycans with terminal NeuAc or NeuGc or without sialic acid. Representative binding specificities for two independent assays for mutant HAs containing mutation A135E and an additional mutation (S128T, I130V, G144R, A159G+A160V, T189A, K193, or A219P) (A) and mutant HAs containing mutations A135E, K193R, and an additional mutation (G144R, A159G+A160V, T189A, or A219P) (B) are shown.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Glycoproteomics, Microarray, Mutagenesis

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Binding specificities of (mutant) HA of A/Turkey/Italy/214845/02 H7N3 to chicken and horse erythrocytes and tracheal epithelium. (A) A hemagglutination assay ( n = 3, mean + standard deviation [SD] shown) with chicken and horse erythrocytes was performed using H7tu WT and mutant HAs (A135E, A135E+S128T, A135E+I130V, and A135E+T189A+K193R). AEC staining was used to visualize tissue binding. Tissue staining of chicken and horse tracheal epithelium was performed with WT and Y161A mutant HA of A/Vietnam/1203/2004 H5N1 as a positive and negative control (B) and H7tu WT or mutant HAs as described for panel A (C).

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Mutagenesis, Hemagglutination Assay, Standard Deviation, Staining, Negative Control

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Evaluation of the binding specificities of the (mutant) HA of A/Chicken/Jalisco/12283/12 H7N3. (A) Alignment of the RBS of the HAs of A/Turkey/Italy/214845/02 H7N3 and A/Chicken/Jalisco/12283/12 H7N3, with the amino acid positions indicated above the alignment and dots indicating identical amino acids. A full alignment of the HAs is shown in Fig. S1. (B) The binding specificities of WT HA of A/Chicken/Jalisco/12283/12 H7N3 and A135E, S128T+A135E, I130V+A135E, and A135E+T189A+K193R mutant HAs were evaluated on the glycan microarray as described in the legend to . (C) Binding specificities of WT and mutant HAs were further tested in a hemagglutination assay on chicken and horse erythrocytes ( n = 3, mean + SD shown). (D) The binding of the WT and mutant HAs to chicken and horse tracheal epithelium (controls shown in ) is visualized using AEC staining.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Mutagenesis, Glycoproteomics, Microarray, Hemagglutination Assay, Staining

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Effect of the combination of the 5 mutations at positions 128, 130, 135, 189, and 193 in A/Turkey/Italy/214845/02 H7N3 and A/Equine/New York/43/73 H7N7 HA. (A to C) The binding specificity of the mutant HA (S128T, I130V, A135E, T189A, K193R) of A/Turkey/Italy/214845/02 H7N3 was evaluated by using the glycan microarray as described in the legend to (A), by the hemagglutination assay with chicken and horse erythrocytes ( n = 3, mean and SD shown) (with H5 NeuAc and NeuGc controls shown in ) (B), and by immunohistochemistry using chicken and horse tracheal epithelium (controls shown in ), visualized using AEC staining (C). (D to F) Likewise, the binding specificities of the WT and mutant (T128S, V130I, E135A, A189T, R189K) HAs of A/Equine/New York/43/73 H7N7 were evaluated by using the glycan microarray in which the WT had been previously investigated (D), the hemagglutination assay (E), and tissue staining (F).

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Mutagenesis, Glycoproteomics, Microarray, Hemagglutination Assay, Immunohistochemistry, Staining

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Phylogenetic tree of equine and avian H7 HA sequences and evaluation of the binding specificities of mutants of the HA of A/Turkey/Italy/214845/02 H7N3 at amino acid position 135. Phylogenetic trees of equine and avian H7 IAV strains from the Eurasian lineage were reconstructed. The equine H7 strains cluster as a single monophyletic clade. The avian strains that are most closely related to the equine strains (A/FPV/Dutch/1927 H7N7 and A/Turkey/England/1963 H7N3) are indicated, as well as A/Equine/New York/43/73 H7N7. The annotated phylogenetic tree with all strain names is shown in Fig. S2. The variation in amino acids at positions 135 (alanine, threonine, glutamic acid, valine) (A), 128 (serine, threonine, asparagine) (B), 130 (isoleucine, valine) (C), 189 (threonine, alanine, aspartic acid, glycine) (D), and 193 (lysine, arginine) (E) is shown. For all positions, the amino acid of the predicted most recent common ancestor (MRCA) is shown. (F) Representative binding specificities on the glycan microarray (as described in the legend to ) for H7tu A135T and A135V mutants are shown.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Glycoproteomics, Microarray

Journal: Journal of Virology

Article Title: N -Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses

doi: 10.1128/jvi.02120-21

Figure Lengend Snippet: Evaluation of the binding specificities of the (mutant) HA of A/Duck/Australia/341/1983 H15N8. (A) Alignment of the RBS of the HAs of A/Turkey/Italy/214845/02 H7N3 and A/Duck/Australia/341/1983 H15N8, with the amino acid positions indicated above the alignment and dots indicating identical amino acids. A full alignment of the HAs is shown in Fig. S1. (B) The binding specificities of WT HA of A/Duck/Australia/341/1983 H15N8 and A135E, S128T+I130V+A135E, A135E+T189A+K193R, and S128T+I130V+A135E+T189A+K193R mutant Has were evaluated on the glycan microarray as described in the legend to . (C) Binding specificities of WT and mutant HAs were further tested in a hemagglutination assay on chicken and horse erythrocytes ( n = 3, mean + SD shown). (D) Binding of the WT and mutant HAs to chicken and horse tracheal epithelium (controls shown in ) is visualized using AEC staining.

Article Snippet: HA-encoding cDNAs of A/Turkey/Italy/214845/02 H7N3 ( ) (synthesized and codon optimized by GenScript), A/Chicken/Jalisco/12283/12 H7N3 (a kind gift from Florian Krammer, Mt.

Techniques: Binding Assay, Mutagenesis, Glycoproteomics, Microarray, Hemagglutination Assay, Staining