Journal: Virology Journal

Article Title: Identification of linear B cell epitopes on the E146L protein of African swine fever virus with monoclonal antibodies

doi: 10.1186/s12985-024-02570-0

Figure Lengend Snippet: Preliminary epitope mapping of mAbs. ( A ) The outer-membrane domain of the E146L protein was truncated into seven short peptides 30 amino acids in length with 15 amino acids overlapping. IMD: internal membrane domain, TMD: transmembrane domain. ( B ) The peptides were expressed as MBP fusion proteins in Escherichia coli and verified by SDS‒PAGE. The peptide fusion proteins were used to map the epitopes of the mAbs by ELISA ( C , E and G ) and western blotting ( D , F and H ). The results revealed that the mAb 12H12 recognized peptides P1 and P2, and the mAbs 15G1 and 15H10 identified peptides P7 and P1, respectively

Article Snippet: Six transmembrane proteins of ASFV (I329L, E146L, C257L, EP153R, I177L, and F165R) were selected through the transmembrane protein prediction online tool ( https://services.healthtech.dtu.dk/services/TMHMM-2.0/ ).

Techniques: Membrane, Enzyme-linked Immunosorbent Assay, Western Blot

Journal: Microbiology and Molecular Biology Reviews : MMBR

Article Title: Physiological and Molecular Understanding of Bacterial Polysaccharide Monooxygenases

doi: 10.1128/MMBR.00015-17

Figure Lengend Snippet: Bacterial sensing of cellulose and chitin. Bacteria can sense cellulose and chitin through CebR and DasR, respectively. In turn, CebR and DasR regulate the expression of PMOs and other GHs. PMOs cleave cellulose and chitin chains, generating new chain ends more readily accessible by GHs for further degradation.

Article Snippet: The Pfam hidden Markov model for bacterial PMOs can be found under accession number PF03067 ( 75 , 76 ), and it can also be accessed under InterPro database accession number IPR004302 .

Techniques: Bacteria, Expressing

Journal: Microbiology and Molecular Biology Reviews : MMBR

Article Title: Physiological and Molecular Understanding of Bacterial Polysaccharide Monooxygenases

doi: 10.1128/MMBR.00015-17

Figure Lengend Snippet: Sequence alignment of conserved regions of bacterial PMOs. Green highlighting shows copper-coordinating residues, gray highlighting shows conserved residues on the putative substrate binding surface, and purple highlighting shows a conserved aromatic residue by the active site. Numbers indicate the residue of the reference sequence (italics). Shown are bacterial PMOs predicted to oxidize C-1 of cellulose (A), C-1/C-4 of cellulose (B), and chitin (C).

Article Snippet: The Pfam hidden Markov model for bacterial PMOs can be found under accession number PF03067 ( 75 , 76 ), and it can also be accessed under InterPro database accession number IPR004302 .

Techniques: Sequencing, Binding Assay, Residue

Journal: Microbiology and Molecular Biology Reviews : MMBR

Article Title: Physiological and Molecular Understanding of Bacterial Polysaccharide Monooxygenases

doi: 10.1128/MMBR.00015-17

Figure Lengend Snippet: Putative functions of bacterial PMOs. Following secretion, bacterial PMOs can oxidize a range of polysaccharide substrates, resulting in PMOs being implicated as having various functions, including degrading biomass, being involved in endosymbiotic relationships, and serving as virulence factors of pathogenic bacteria and as antifungal agents, in addition to providing a nutritional source for bacteria.

Article Snippet: The Pfam hidden Markov model for bacterial PMOs can be found under accession number PF03067 ( 75 , 76 ), and it can also be accessed under InterPro database accession number IPR004302 .

Techniques: Bacteria