Phage Hunters Spring 2017
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
|---|
| 9VIRU:W0M2E9 | 2017-04-23 09:21:52 CDT | GO:0003796 lysozyme activity (F) | PMID:27656173 | ECO:0000314 direct assay evidence used in manual assertion | Figure 3 shows antibacterial (lytic) activity of LysABP-01
| challenge |
| 9CAUD:R4IQ32 | 2017-04-23 09:30:54 CDT | GO:0003796 lysozyme activity (F) | PMID:27656173 | ECO:0000247 sequence alignment evidence used in manual assertion | Figure 1 shows that PlyAB1 (R4IQ32) is a homologue of LysABP-01 (accession no: W0M2E9) and
LysAB2 (accession no: F1BCP4) whose endolysin activity have been demonstrated in
PMID:27656173 [LysABP-01 (accession no: W0M2E9)] and PMID:21264466 [LysAB2 (accession no: F1BCP4)]
| challenge |
| 9CAUD:Q7Y3F1 | 2017-04-23 09:55:14 CDT | GO:0003796 lysozyme activity (F) | PMID:16818874 | ECO:0000315 mutant phenotype evidence used in manual assertion | FIGURE 6 shows that PlyCA contains a functional Cysteine, Histidine-Dependent Amidohydrolase Peptidase
(CHAP) Domain confirming it to have amidase activity, because it is able to cleave the amide bond between
N-acetyl muramic acid and L-alanine in the streptococcal peptidoglycan (Fischetti et al., 1972).
| challenge |
| 9CAUD:R9VY83 | 2017-04-23 12:14:46 CDT | GO:0008745 N-acetylmuramoyl-L-alanine amidase activity (F) | PMID:26167894 | ECO:0000314 direct assay evidence used in manual assertion | The authors claim that 'BlastP, Pfam and HHpred identified an N-acetylmuramoyl-L-alanine
amidase belonging to the Amidase_2 family (Pfam 01510) at the N-terminus
encompassing two third of the protein. CDD database identified 5 putative amidase catalytic
residues: two histidines (position 29 and 129), a phenylalanine (position 53), a lysine (position
135) and a cysteine (position 137)' (First paragraph of the results section).
Table 2 however confirmed that PlyPl23 has lytic activity and also shows the lytic spectrum of PlyPl23
when assessed against a panel of 20 P. larvae isolates and 4 additional strains belonging
to other related bacterial species (Bacillus cereus, Lactobacillus paracasei,
Lactobacillus pentosus, Bacillus subtilis), and compared with that of the respective phage phiIBB_Pl23.
Results showed that while the phage phiIBB_Pl23 was able to lyse 16 of the 20 strains (80%),
its endolysin (PlyPl23) was active against all the tested Paenibacillus larvae strains.
The Bacillus and Lactobacillus strains were not lysed by the phage or by the enzyme
| challenge |
| 9CAUD:I1TLF9 | 2017-04-23 12:24:05 CDT | GO:0009253 peptidoglycan catabolic process (P) | PMID:25595773 | ECO:0000314 direct assay evidence used in manual assertion | Figure 6 shows that LysPBC1 is a putative N-acetylmuramoyl-L-alanine amidase consisting of
an N-terminal type 3 amidase domain (PF01520) and a C-terminal amidase02_C domain (PF12123).
Table 1 shows that when purified LysPBC1 was added exogenously it lysed all strains of
B. cereus group bacteria, including B. cereus, B. thuringiensis, B. mycoides, and B. weihenstephanensis,
| challenge |
| 9CAUD:Q7Y4H8 | 2017-04-23 13:26:18 CDT | GO:0099613 protein targeting to cell wall (P) | PMID:24267666 | ECO:0000314 direct assay evidence used in manual assertion | Figure 1 and 3 show that purified proteins from all C-terminal (Cell Wall Binding [CBD])
- Green Flourescent Protein (GFP)fusion constructs, had evident binding
activity. In all cases, no binding activity of unfused GFP, used as a negative control, was detected.
| challenge |
| requireschanges | 9CAUD:A0A0K2CYE7 | 2017-04-26 00:18:26 CDT | GO:0009253 peptidoglycan catabolic process (P) | PMID:26904379 | ECO:0000314 direct assay evidence used in manual assertion | Figures 3, 4 and 5 show PlyPalA has lytic activity on P. larvae cells.
Table 1 showed that PlyPalA had lytic activity against different P. larvae genotypes
and the lytic activity varied from genotype-to-genotype.
ERIC genotype I members were the most susceptible to PlyPalA lytic activity
| challenge |
| 9CAUD:K7NPX3 | 2017-04-28 01:48:50 CDT | GO:0004175 endopeptidase activity (F) | PMID:27766357 | ECO:0000314 direct assay evidence used in manual assertion | Figure 4 AND S4 show the digestion of E. coli peptidoglycan sacculus KP27 endolysin and shows
that KP27 endolysin is a l-alanyl-d-glutamate endopeptidase. It further shows that
KP27 endolysins has an endopeptidase activity cleaving between l-Ala and d-Glu of the stem
peptide and no d-alanyl-d-alanine carboxypeptidase activity.
| challenge |
| 9CAUD:D5JFH4 | 2017-04-28 03:49:35 CDT | GO:0004175 endopeptidase activity (F) | PMID:2776635 | ECO:0000247 sequence alignment evidence used in manual assertion | The predicted endolysin (ADE34958) of phage KP15 is very similar to the endolysin (AEX26632) of phage KP27.
The only difference is only in one amino acid (glutamic acid of KP15 endolysin is replaced by glutamine
in the KP27 endolysin in the seventeenth position from N-terminus) (results section, subsection;
Description of KP15 and KP27 lysis system).
Figure 4 AND S4 show the digestion of E. coli peptidoglycan sacculus KP27 endolysin and shows
that KP27 endolysin is a l-alanyl-d-glutamate endopeptidase. It further shows that
KP27 endolysins has an endopeptidase activity cleaving between l-Ala and d-Glu of the stem
peptide and no d-alanyl-d-alanine carboxypeptidase activity.
| challenge |
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