INT321105

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Context Info
Confidence 0.00
First Reported 2010
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 1
Total Number 5
Disease Relevance 1.69
Pain Relevance 0

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extracellular space (F5) mitochondrion (DBT) extracellular region (F5)
small molecule metabolic process (DBT) cell adhesion (F5) plasma membrane (F5)
DBT (Homo sapiens)
F5 (Homo sapiens)
Pain Link Frequency Relevance Heat
headache 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Togavirus Infection 615 100.00 Very High Very High Very High
Infection 25 5.00 Very Low Very Low Very Low
Sprains And Strains 15 5.00 Very Low Very Low Very Low
Disease 10 5.00 Very Low Very Low Very Low
Hepatitis A Virus Infection 10 5.00 Very Low Very Low Very Low
Viral Meningitis 10 5.00 Very Low Very Low Very Low
Measles 5 5.00 Very Low Very Low Very Low
Dengue 5 5.00 Very Low Very Low Very Low
Communicable Diseases 5 5.00 Very Low Very Low Very Low
Acquired Immune Deficiency Syndrome Or Hiv Infection 5 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Further analysis revealed that F5 neutralized all four mMAb neutralization-escape variant viruses to the same degree as the parent VEEV TC-83, indicating that binding of F5 was not affected by an aa change at either E2-182, -183, -199 or -207, providing important evidence that F5 recognized a different E2 epitope than any of the four neutralizing mMAbs used to generate the variant viruses (Table 5).
E2 Binding (recognized) of F5 associated with togavirus infection
1) Confidence 0.00 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.22 Pain Relevance 0
These analyses indicate that F5 nIgG does not bind to an epitope within the major neutralization domain on the VEEV E2 glycoprotein defined by mMAbs [33].


E2 Neg (not) Binding (bind) of F5 nIgG associated with togavirus infection
2) Confidence 0.00 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.35 Pain Relevance 0
If the epitope recognized by F5 were the same as, or near, any of the changed aa residues (E2-182, 183, 199, and 207) in the neutralization-escape variant viruses, then F5 would be unable to neutralize that variant.
E2 Binding (recognized) of F5
3) Confidence 0.00 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.46 Pain Relevance 0
Based on the aa changes in the variant viruses, F5 binding was mapped to aa residues E2-115 to 119 (Table 7).
E2 Binding (binding) of F5
4) Confidence 0.00 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.21 Pain Relevance 0
Mapping of this epitope to a unique E2 neutralization site was based on the data presented in this study: (1) epitope binding by hMAb F5 nIgG was more sensitive to 0.3% BPL treatment than epitopes recognized by neutralizing mMAbs, (2) hMAb F5 was able to neutralize all anti-VEEV mMAb neutralization escape variant viruses and therefore did not bind to E2 residues 182–207, defined as the “critical” neutralization domain, and (3) hMAb F5 neutralization escape variant viruses vF5-3 and vF5-5 defined a neutralization epitope involving E2 aa115–119.
E2 Neg (not) Binding (bind) of hMAb F5 associated with togavirus infection
5) Confidence 0.00 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.45 Pain Relevance 0

General Comments

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