| Challenge | AHutchison,
Team Purple A 2018 | 2018-04-03 20:36:49 CDT | I agree with most of this annotation. However, if you are going with IDA I would take out the part of your annotation where you discuss figure 2 and how the mutant SPP1sus82 led to assembly of DNA filled heads and tails because that makes me think that this should be labeled IMP. Other than that, this is great.
| None, yet. |
Public
Assessment | Ivanerill | 2018-04-30 05:06:41 CDT | No notes given. | Acceptable
✔ Protein
✔ Publication
✔ Qualifier
✔ Go term
✔ Evidence
✔ With/From
✔ Notes
✔ Unique/Original
|
Public
Assessment | DanielRenfro | 2018-04-19 13:46:57 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0098005 |
viral head-tail joining |
PMID:24443902 |
IDA: Inferred from Direct Assay |
|
P |
An in-vitro complementation assay was used to study incorporation of gp17 during assembly of viral particles. Each extract was separately mixed with 4 different components; water, complete tails purified from SPP1sus31 with gp17, tails without gp17 purified from SPP1sus82, and purified gp17. After incubation, the titer of the progeny was calculated in Figure 7. The expected result was sus31 tails in both extracts allowed it to join to the capsids for virion assembly. When mixing SPP1sus82 tails without gp17 with SPP1sus45, virion particles assembled, suggesting endogenous gp17 was able to join head and tail. SPP1sus82 had a low titer, thus tails weren’t able to attach. Finally, purified gp17 mixed SPP1sus82 extracts was sufficient for tail to head stickage. This assay shows that gp17 is involved in binding to the tail and later attaching to the DNA-filled capsid. |
complete
CACAO 13181
| on BPSPP:TUBE
| Flagged
|
Public
Assessment | Ivanerill | 2018-04-15 15:17:00 CDT | You have a mix of evidence in your notes. Determine which one (IDA or IMP) more conclusively supports your annotation and make that explicit in your notes.
| Requires Changes
✔ Protein
✔ Publication
✔ Qualifier
✔ Go term
✗ Evidence
✔ With/From
✗ Notes
✔ Unique/Original
|
Public
Assessment | DanielRenfro | 2018-04-08 20:47:10 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0098005 |
viral head-tail joining |
PMID:24443902 |
IDA: Inferred from Direct Assay |
|
P |
An in-vitro complementation assay was used to study incorporation of gp17 during assembly of infectious particles in infected cells. The extracts were prepared from lysates of bacteria infected with SPP1 mutants blocked in tail-to-head joining (SPP1sus82) and tail tube protein deficient mutants (SPP1sus45). Each extract was separately mixed with 4 different components; water, complete tails purified from SPP1sus31 with gp17, tails without gp17 purified from SPP1sus82, and purified gp17. After incubation, the titer of the progeny was calculated in Figure 7. The expected result was sus31 tails in both extracts allowed it to join to the capsids for virion assembly. When mixing SPP1sus82 tails without gp17 with SPP1sus45, virion particles assembled, suggesting endogenous gp17 was able to join head and tail. SPP1sus82 had a low titer, thus tails weren’t able to attach. Finally, purified gp17 mixed SPP1sus82 extracts was sufficient for tail to head stickage. This assay shows that gp17 is involved in binding to the tail and later attaching to the DNA-filled capsid. |
complete
CACAO 13181
| on BPSPP:TUBE
| Flagged
|
