The DOI matches its Crossref record.
An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications
Abstract
Tropomyosin (TM) is a major allergen in crustaceans, which often causes allergy and is fatal to some consumers. Currently, the most effective treatment is to avoid ingesting TM, although most adverse events occur in accidental ingestion. In this review, the molecular characterization, epitopes, cross‐reactivity, and pathogenesis of TM are introduced and elucidated. Modification of TM by traditional processing methods such as heat treatment and enzymatic hydrolysis, and innovative processing technologies including high‐pressure treatment, cold plasma (CP), ultrasound, pulsed electric field (PEF), pulsed ultraviolet, microwave and irradiation are discussed in detail. Particularly, enzymolysis, PEF, and CP technologies show great potential for modifying TM and more studies are needed to verify their effectiveness for the seafood industry. Possible mechanisms and the advantages/disadvantages of these technologies for the mitigation of TM allergenicity are also highlighted. Further work should be conducted to investigate the allergenicity caused by protein segments such as epitopes, examine the interaction sites between the allergen and the processing techniques and reveal the reduction mechanism of allergenicity.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The homology between Ascaris tropomyosin and mite tropomyosins, including Der p 10 and Blo t 10, may contribute to cross-reactive IgE responses and complicate the interpretation of dust mite sensitization in parasite-exposed individuals (Cheng et al. 2022; Shafique et al. 2012; Sousa-Santos et al. 2020).”
From Parasites and allergies: a complex bidirectional relationship from evolutionary origins to modern therapeutics (2026) · cites this paper as Cheng et al. 2022
In the citing paper
“Tropomyosins may be involved in cross-reactions between crustaceans, mollusks, dust mites, cockroaches, and nematodes such as Ascaris lumbricoides (Asc l 3).”
From Parasites and allergies: a complex bidirectional relationship from evolutionary origins to modern therapeutics (2026) · cites this paper as Cheng et al. 2022
In the citing paper
“Tropomyosins are among the most important examples of cross-reactive invertebrate allergens. They are characterized by high thermostability, resistance to digestion, and strong structural conservation across different invertebrate species.”
From Parasites and allergies: a complex bidirectional relationship from evolutionary origins to modern therapeutics (2026) · cites this paper as Cheng et al. 2022
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 143
- 10.1034/j.1398-9995.2001.056006478.x · DOI
- 10.1371/journal.pone.0067487 · DOI
- 10.1021/acs.jafc.0c02366 · DOI
- 10.1016/j.ultsonch.2018.09.016 · DOI
- 10.1016/j.foodchem.2021.129195 · DOI
- 10.1111/ijfs.14600 · DOI
- 10.1016/j.foodchem.2021.131162 · DOI
- 10.1016/j.aller.2019.06.005 · DOI
- 10.1016/j.tifs.2020.07.008 · DOI
- 10.1016/j.tifs.2021.03.045 · DOI
- 10.1016/j.ultsonch.2020.105293 · DOI · Paper page
- 10.1111/1541-4337.12670 · DOI
- 10.1080/10408398.2017.1356264 · DOI
- 10.3390/foods9081134 · DOI
- 10.1038/s41598-019-51535-9 · DOI
- 10.1080/10408398.2019.1654429 · DOI
- 10.1016/j.tifs.2020.07.022 · DOI
- 10.1111/jam.14823 · DOI
- 10.1016/j.foodchem.2019.126133 · DOI
- 10.1007/s12016-020-08826-1 · DOI
- 10.3390/molecules25040954 · DOI
- 10.1016/j.jaip.2019.10.019 · DOI
- 10.3389/fimmu.2020.00442 · DOI
- 10.1080/10408398.2020.1722942 · DOI
- 10.1016/j.foodchem.2020.127811 · DOI
- 10.1186/s12948-021-00142-z · DOI
- 10.1016/j.tifs.2018.01.007 · DOI
- 10.1016/j.foodchem.2018.09.113 · DOI
- 10.1016/j.foodchem.2019.125143 · DOI
- 10.1080/10408398.2020.1735297 · DOI
- 10.1016/j.ultsonch.2021.105609 · DOI
- 10.1016/j.ultsonch.2021.105660 · DOI
- 10.1016/j.foodcont.2019.04.044 · DOI
- 10.1002/jsfa.9071 · DOI
- Fu L., 2019, Food processing to eliminate food allergens and development of hypoallergenic foods, 123
- 10.1016/j.tifs.2019.03.025 · DOI
- 10.1021/acs.jafc.7b06042 · DOI
- 10.1016/j.radphyschem.2021.109369 · DOI
- 10.1016/j.foodchem.2014.10.063 · DOI
- 10.1080/10408398.2019.1584600 · DOI
- 10.1007/s11033-014-3534-6 · DOI
- 10.1016/j.foodchem.2018.05.051 · DOI
- 10.1016/j.jff.2019.103634 · DOI
- 10.1080/10408398.2018.1555131 · DOI
- 10.1016/j.tifs.2018.02.017 · DOI
- 10.1016/j.foodchem.2020.128461 · DOI
- 10.1016/j.ultsonch.2019.104950 · DOI
- 10.1111/all.13956 · DOI
- 10.1016/j.fct.2010.02.010 · DOI
- 10.1016/j.str.2018.05.002 · DOI
- 10.1016/j.tifs.2020.02.009 · DOI
- 10.1016/j.fct.2014.12.002 · DOI
- 10.1002/mnfr.201300584 · DOI
- 10.1016/j.foodchem.2013.06.105 · DOI
- 10.1080/10408398.2018.1471658 · DOI
- 10.1111/cea.13503 · DOI
- 10.18176/jiaci.0381 · DOI
- 10.1016/j.foodchem.2016.03.043 · DOI
- 10.21077/ijf.2019.66.3.88139-14 · DOI
- 10.1002/jsfa.8221 · DOI
- 10.2500/aap.2019.40.4249 · DOI
- 10.1111/jfpe.12262 · DOI
- 10.17221/242/2009-CJFS · DOI
- 10.1016/j.foodchem.2019.125575 · DOI
- 10.1002/jsfa.2746 · DOI
- 10.1007/s00217-005-0246-0 · DOI
- 10.1021/acs.jafc.8b01967 · DOI
- 10.1021/acs.jafc.6b05816 · DOI
- 10.1111/j.1750-3841.2009.01391.x · DOI
- 10.1002/jsfa.4167 · DOI
- 10.1021/acs.jafc.8b03466 · DOI
- 10.1039/D0FO02869J · DOI
- 10.1016/j.foodchem.2020.128735 · DOI
- 10.1016/j.lwt.2020.109370 · DOI
- 10.1080/09540105.2016.1251394 · DOI
- 10.1016/j.ifset.2015.03.002 · DOI
- 10.1111/pai.13493 · DOI
- 10.1007/s40629-016-0124-2 · DOI
- 10.18176/jiaci.0355 · DOI
- 10.1016/j.foodres.2020.109997 · DOI
- 10.3390/pharmacy7030122 · DOI
- 10.1016/j.biochi.2020.03.013 · DOI
- 10.1016/j.radphyschem.2019.108525 · DOI
- 10.1016/j.ifset.2016.06.007 · DOI
- 10.1080/09540105.2017.1323187 · DOI
- 10.1016/j.foodchem.2019.125186 · DOI
- 10.1016/j.anai.2016.07.015 · DOI
- 10.3136/fstr.20.955 · DOI
- 10.1007/s13197-018-3104-3 · DOI
- 10.1016/B978-0-12-804581-7.00011-7 · DOI
- 10.3390/foods10020409 · DOI
- 10.1002/mnfr.201900923 · DOI
- 10.1007/s11947-019-02382-z · DOI
- 10.1016/j.lwt.2019.05.041 · DOI
- 10.1111/1541-4337.12474 · DOI
- 10.1016/j.lwt.2019.108635 · DOI
- 10.1080/10408398.2020.1776210 · DOI
- Peixoto S., 2017, Tropomyosin from vertebrates as an allergen—Case report, Allergy, 72, 534
- 10.1080/10408398.2021.1904822 · DOI
- 10.1080/07315724.2015.1014120 · DOI
- 10.1016/j.tifs.2016.01.001 · DOI
- 10.1016/j.humimm.2013.08.276 · DOI
- 10.1002/mnfr.201800148 · DOI
- 10.1111/1750-3841.12169 · DOI
- 10.1016/j.molimm.2018.04.008 · DOI
- 10.1111/all.14574 · DOI
- 10.1021/acs.biochem.0c00203 · DOI
- 10.1016/j.cej.2017.05.178 · DOI
- 10.1146/annurev-food-030117-012517 · DOI
- 10.1016/j.procbio.2014.07.005 · DOI
- 10.3390/ijerph8072569 · DOI
- Shriver S. K.(2011b). Effect of selected nonthermal processing methods on the allergen reactivity of Atlantic white shrimp (Litopenaeus setiferus) (master's thesis). University of Florida Gainesville FL.
- 10.1016/j.jaci.2017.11.003 · DOI
- 10.1016/B978-0-12-815251-5.00008-6 · DOI
- Singh P. K. &Huppertz T.(2020).Effect of nonthermal processing on milk protein interactions and functionality. In M. Boland & H. Singh (Eds) Milk Proteins(pp. 293–324). Elsevier. · DOI
- 10.3390/ijms21031012 · DOI
- 10.2147/JAA.S142476 · DOI
- 10.1111/cod.13130 · DOI
- 10.1080/10408398.2015.1045965 · DOI
- Verhoeckx K. C. M. Vissers Y. M. Baumert J. L. Faludi R. Feys M. Flanagan S. Herouet‐Guicheney C. Holzhauser T. Shimojo R. van der Bolt N. Wichers H. & Kimber I. (2015). Food processing and allergenicity.Food and Chemical Toxicology 80 223‐240. · DOI · Paper page
- 10.1016/j.ifset.2019.02.001 · DOI
- 10.1016/j.foodres.2019.108942 · DOI
- 10.1002/jsfa.11177 · DOI
- 10.1016/j.ultsonch.2020.105409 · DOI
- 10.4168/aair.2016.8.2.101 · DOI
- 10.1002/ppap.201900219 · DOI
- 10.1002/jsfa.10926 · DOI
- 10.1016/j.foodchem.2020.126763 · DOI
- 10.1007/s12010-011-9534-2 · DOI
- 10.1016/j.fct.2010.11.046 · DOI
- 10.1038/nri.2016.111 · DOI
- 10.1016/j.foodchem.2016.09.139 · DOI
- 10.1016/j.foodchem.2013.10.154 · DOI
- Zhang Y., 2015, AFM and NMR imaging of squid tropomyosin Tod p1 subjected to high hydrostatic pressure: evidence for relationships among topography, characteristic domain and allergenicity, Royal Society of Chemistry Advances, 5, 73207
- 10.1515/ijfe-2018-0392 · DOI
- 10.1080/09540105.2017.1387520 · DOI
- 10.1016/j.foodchem.2017.11.072 · DOI
- 10.1016/j.foodchem.2019.125603 · DOI
- 10.1039/D0FO03039B · DOI
- 10.1016/j.foodcont.2019.02.041 · DOI
- Zhu Z. Zhou Q. & Sun D.‐W. (2019). Measuring and controlling ice crystallization in frozen foods: A review of recent developments.Trends in Food Science & Technology 90 13–25. · DOI
- Zhu H. Cheng J.‐H. Han Z. & Han Z. (2021). Cold plasma enhanced natural edible materials for future food packaging: structure and property of polysaccharides and proteins‐based films.Critical Reviews in Food Science and Nutrition.https://doi.org/10.1080/10408398.2021.2002258 · DOI
- Zhu H. Han Z. Cheng J.‐H. & Sun D.‐W (2022). Modification of cellulose from sugarcane (Saccharum officinarum) bagasse pulp by cold plasma: Dissolution structure and surface chemistry analysis.Food chemistry 374 131675. · DOI
Cited by
Sorted by citations
Packi, K., Świerczewski, D., Klimczak, S., Ochab, D., Gałęziewska, J., Gromek, P., Kruczkowska, W., Płuciennik, E., Kałuzińska-Kołat, Ż., & Kołat, D. (2026) · Antonie van Leeuwenhoek · doi:10.1007/s10482-026-02425-4
Metadata
- Authors
- Cheng, J., Wang, H., & Sun, D.
- Venue
- Comprehensive Reviews in Food Science and Food Safety
- Publisher
- Wiley
- Published
- 2021-12-26
- Volume
- 21
- Issue
- 1
- Pages
- 127-147
- ISSN
- 1541-4337
- Cited by
- 86
- References
- 0
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
