Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
111-170 |
DRI_Background |
denotes |
Fish are the largest and most diverse group of vertebrates. |
T2 |
171-272 |
DRI_Approach |
denotes |
Fish are also a part of the eight food groups that cause the majority of IgE mediated food reactions. |
T3 |
273-450 |
DRI_Background |
denotes |
Detection tools for fish allergens are however limited due to the great diversity of fish species, despite fish allergy and its major allergen parvalbumin being well documented. |
T4 |
451-534 |
DRI_Background |
denotes |
The most commonly studied fish are frequently consumed in North America and Europe. |
T5 |
535-659 |
DRI_Background |
denotes |
However, much less is known about fish allergens in the Australasian region although fish is widely consumed in this region. |
T6 |
660-873 |
DRI_Background |
denotes |
A comprehensive phylogenetic analysis was performed of known parvalbumin amino acid sequences to determine possible candidate antigens for new cross-reactive antibodies to be used to detect most fish parvalbumins. |
T7 |
874-1029 |
DRI_Background |
denotes |
Polyclonal rabbit antibodies were raised against parvalbumins from frequently consumed barramundi (Lates calcarifer), basa (Pangasius bocourti), pilchard ( |
T8 |
1044-1080 |
DRI_Background |
denotes |
) and Atlantic salmon (Salmo salar). |
T9 |
1081-1189 |
DRI_Approach |
denotes |
These were evaluated for cross-reactivity against a panel of 45 fish extracts (raw, heated and canned fish). |
T10 |
1190-1205 |
REPLACED |
denotes |
Anti-barramundi |
T11 |
1218-1358 |
DRI_Background |
denotes |
proved to be the most cross-reactive antibody, detecting 87.5% of the 40 species analyzed, followed by anti-pilchard and anti-basa antibody. |
T12 |
1359-1466 |
DRI_Outcome |
denotes |
In contrast the anti-salmon antibody was very specific and only reacted to salmonidae and a few other fish. |
T13 |
1467-1601 |
DRI_Outcome |
denotes |
All analyzed fish species, except mahi mahi, swordfish, yellowfin tuna and all 5 canned fish had parvalbumin detected in raw extracts. |
T14 |
1602-1822 |
DRI_Background |
denotes |
However antibody reactivity to many fish was heat liable or susceptible to denaturation, demonstrating that some parvalbumins have most likely conformational epitopes, which lose antibody reactivity after heat treatment. |
T15 |
1823-1868 |
DRI_Outcome |
denotes |
We have demonstrated the generation of highly |
T16 |
1901-2010 |
DRI_Outcome |
denotes |
antibodies that could be used for the detection of allergenic fish parvalbumin in contaminated food products. |
T17 |
2011-2183 |
DRI_Background |
denotes |
This cross-reactivity study thus shows processing of fish, especially canning, can have on impact on antibody recognition by ELISA, possibly similar to IgE-binding in vivo. |