PMID- 18521668
OWN - NLM
STAT- MEDLINE
DCOM- 20090115
LR  - 20211020
IS  - 1436-2228 (Print)
IS  - 1436-2228 (Linking)
VI  - 10
IP  - 6
DP  - 2008 Nov-Dec
TI  - Identification of tropomyosins as major allergens in antarctic krill and mantis 
      shrimp and their amino acid sequence characteristics.
PG  - 709-18
LID - 10.1007/s10126-008-9109-6 [doi]
AB  - Tropomyosin represents a major allergen of decapod crustaceans such as shrimps 
      and crabs, and its highly conserved amino acid sequence (>90% identity) is a 
      molecular basis of the immunoglobulin E (IgE) cross-reactivity among decapods. At 
      present, however, little information is available about allergens in edible 
      crustaceans other than decapods. In this study, the major allergen in two species 
      of edible crustaceans, Antarctic krill Euphausia superba and mantis shrimp 
      Oratosquilla oratoria that are taxonomically distinct from decapods, was 
      demonstrated to be tropomyosin by IgE-immunoblotting using patient sera. The 
      cross-reactivity of the tropomyosins from both species with decapod tropomyosins 
      was also confirmed by inhibition IgE immunoblotting. Sequences of the 
      tropomyosins from both species were determined by complementary deoxyribonucleic 
      acid cloning. The mantis shrimp tropomyosin has high sequence identity (>90% 
      identity) with decapod tropomyosins, especially with fast-type tropomyosins. On 
      the other hand, the Antarctic krill tropomyosin is characterized by diverse 
      alterations in region 13-42, the amino acid sequence of which is highly conserved 
      for decapod tropomyosins, and hence, it shares somewhat lower sequence identity 
      (82.4-89.8% identity) with decapod tropomyosins than the mantis shrimp 
      tropomyosin. Quantification by enzyme-linked immunosorbent assay revealed that 
      Antarctic krill contains tropomyosin at almost the same level as decapods, 
      suggesting that its allergenicity is equivalent to decapods. However, mantis 
      shrimp was assumed to be substantially not allergenic because of the extremely 
      low content of tropomyosin.
FAU - Motoyama, Kanna
AU  - Motoyama K
AD  - Department of Food Science and Technology, Tokyo University of Marine Science and 
      Technology, Minato-ku, Tokyo, 108-8477, Japan.
FAU - Suma, Yota
AU  - Suma Y
FAU - Ishizaki, Shoichiro
AU  - Ishizaki S
FAU - Nagashima, Yuji
AU  - Nagashima Y
FAU - Lu, Ying
AU  - Lu Y
FAU - Ushio, Hideki
AU  - Ushio H
FAU - Shiomi, Kazuo
AU  - Shiomi K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080603
PL  - United States
TA  - Mar Biotechnol (NY)
JT  - Marine biotechnology (New York, N.Y.)
JID - 100892712
RN  - 0 (Allergens)
RN  - 0 (DNA, Complementary)
RN  - 0 (Tropomyosin)
SB  - IM
MH  - Allergens/genetics/*immunology
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Cross Reactions
MH  - DNA, Complementary/genetics
MH  - Decapoda/genetics/*immunology
MH  - Euphausiacea/genetics/immunology
MH  - Food Hypersensitivity/immunology
MH  - Humans
MH  - Molecular Sequence Data
MH  - Phylogeny
MH  - Sequence Alignment
MH  - Tropomyosin/genetics/*immunology
EDAT- 2008/06/04 09:00
MHDA- 2009/01/16 09:00
CRDT- 2008/06/04 09:00
PHST- 2007/06/18 00:00 [received]
PHST- 2008/04/16 00:00 [accepted]
PHST- 2008/03/25 00:00 [revised]
PHST- 2008/06/04 09:00 [pubmed]
PHST- 2009/01/16 09:00 [medline]
PHST- 2008/06/04 09:00 [entrez]
AID - 10.1007/s10126-008-9109-6 [doi]
PST - ppublish
SO  - Mar Biotechnol (NY). 2008 Nov-Dec;10(6):709-18. doi: 10.1007/s10126-008-9109-6. 
      Epub 2008 Jun 3.