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Warning: mysql_query() [function.mysql-query]: Unable to save result set in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 50
Database error: Invalid SQL: select * from pwn_comment where pid='529940' and iffb='1' order by id limit 0,10
MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select * from pwn_comment where pid='529940' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select * from {P}_comment where pid='529940' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:167] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
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网友点评-Mble of epitope mapping research have reported on fHbp. Pioneering-线缆测高仪,超声波测高仪, 手持式测高仪-上海交通大学科技园上海野豹企业发展公司
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发布于:2018-9-10 15:55:44  访问:113 次 回复: 篇
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Mble of epitope mapping research have reported on fHbp. Pioneering
This function represents an epitope Z-DEVD-FMK Description mappingbased rational style that improved the antigenicity of Ghfp and is in principle applicable to any vaccine candidate whose prospective coverage is limited by sequence variability.Components AND METHODSBacterial strains. Antibody generation. The hybridoma cell line expressing JAR5 (26) was kindly offered by D. M. Granoff PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/25564241 (Children‘s Hospital Oakland Analysis Institute [CHORI]). The murine IgG2b isotype monoclonal antibody JAR5 and also the corresponding Fab fragment had been created and purified by Areta International S.r.l. Subsequently, nuclear magnetic resonance (NMR) (23), hydrogen-deuterium exchange mass spectroscopy (HDX-MS) (24), and X-ray crystallographic studies (25) have permitted exceptional progress in mapping protective epitopes. This details makes members from the fHbp household best candidates for rational design studies attempting to modulate their immunogenicity by the introduction of heterologous epitopes from distinctive variants. To be able to introduce fHbp variant 1-specific epitopes onto Ghfp, we modified the gonococcal protein surface based on the data derived from the NMR epitope mapping on fHbp. We previously mapped by NMR the epitope recognized by the monoclonal antibody 502 (MAb502) precise for fHbp subvariant 1.1 (23). Here, we used the same approach to map the epitope of a second fHbp 1.1-specific monoclonal antibody referred to as JAR5 (26). Each MAb502 and JAR5 have already been reported to induce complement-mediated killing of meningococcal cells within the presence of rabbit complement (22, 26). We decided thus to introduce onto Ghfp each the MAb502 and JAR5 epitopes. Mice immunized with the resulting chimeric proteins elicited serum able to kill a wide panel of meningococcal strains belonging to variants 1, 2, and three. This function represents an epitope mappingbased rational design and style that improved the antigenicity of Ghfp and is in principle applicable to any vaccine candidate whose potential coverage is restricted by sequence variability.Materials AND METHODSBacterial strains. Escherichia coli strains DH5 and BL21(DE3) had been bought from Invitrogen and used as a cloning and expression strain, respectively. Ampicillin (Sigma) was utilized at concentration of 100 g ml 1. Antibody generation. The hybridoma cell line expressing JAR5 (26) was kindly offered by D. M. Granoff PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/25564241 (Children‘s Hospital Oakland Research Institute [CHORI]). The murine IgG2b isotype monoclonal antibody JAR5 along with the corresponding Fab fragment had been produced and purified by Areta International S.r.l. (Gerenzano, Italy). NMR sample preparation and interaction studies. To express recombinant 2H/15N-labeled fHbp subvariant 1.1 for NMR measurements, E. coli BL21(DE3) (pET21b-fHbp) was grown on M9 minimal medium in 80 heavy water (2H2O) with all the addition of glucose and 3.0 g of 15 NH4Cl (98 isotopic enrichment; Sigma-Aldrich) because the sole carbon and nitrogen source, respectively. The culture was induced at A590 of four.0 with 1.four mM sterile filtered isopropyl 1-thio- -D-galactopyranoside (Sigma) for 12 h. The protein lacking the N-terminal leader peptide as well as the lipobox motif and containing a C-terminal six His tag was purified by two chromatographic steps: Ni2 affinity (His-Trap high-performance [HP] 5-ml column; GE Healthcare), and cation exchange (HiTrap SP HP). Analytical gel filtration analysis showed that the recombinant protein was eluted as a monomer.
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