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Order Patatavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Although this is not connected directly with the VLP approach, it is interesting to note here that the chimeric LMV virions tagged with the GFP gene were engineered and used to test the LMV resistance in lettuce (Candresse et al. 2002). The GFP was inserted in frame into the viral polyprotein and was expressed as a translational fusion to the viral helper component protein HC-Pro.
Discovery and characterization of a neutralizing pan-ELR+CXC chemokine monoclonal antibody
Published in mAbs, 2020
Jeffrey S. Boyles, Catherine B. Beidler, Beth A. Strifler, Daniel S. Girard, Zhanna Druzina, Jim D. Durbin, Michelle L. Swearingen, Linda N. Lee, Kristine Kikly, Sudhakar Chintharlapalli, Derrick R. Witcher
Aside from the ELR motif and the N-loop, several additional key contacts are observed. Both chemokine disulfides are contacted directly with a hydrogen bond between the HC Asn59 sidechain and the chemokine Cys7/Cys34 disulfide and multiple contacts <4.5 Å between both the HC Tyr104 backbone and the HC Pro106 and the chemokine Cys9/Cys50 disulfide (Figure S5). In all four structures, the HC Ser55 and/or HC Ser57 sidechain hydrogen bonds to a polar/charged amino acid in the same position in the chemokine: Gln37 in cCXCL2, Glu37 in cCXCL3, Gln33 in cCXCL7, and Asn36 in hCXCL8. A complete list of observed hydrogen bonding demonstrates several key conserved contacts, but also the overall plasticity of LY3041658 and its ability to recognize the diverse sequences in the ELR+CXC chemokine family (Table S6). The long HC CDR3 loop has several exposed hydrophobic residues (Tyr104, Tyr105, Pro106) that extend away from the antibody surface and interact with numerous conserved hydrophobic chemokine amino acids that were also identified by alanine scanning: Tyr104 with Leu15 in cCXCL2/3, Thr11 in cCXCL7, and Tyr13 in hCXCL8; Tyr105 with Ala50 in cCXCL2/3, Ile46 in cCXCL7, and Leu49 in cCXCL8; and Pro106 with Ile41 in cCXCL2/3, Ile37 in cCXCL7, Ile40 in hCXCL8 (Figure 7(d)). The hCXCL8 Phe17, Glu38, and Leu51, which were identified by alanine scanning, are not observed in the LY3041658 binding interface, and therefore are instead likely important for conformation rather than part of the epitope. These positions are indicated in sequence alignment across the human, cynomolgus monkey, mouse, and rat chemokines in Figure S6, highlighting the diversity of sequences that LY3041658 is able to recognize.