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Cited by 110Genetically Modified Organisms ResearchAgricultural safety and regulationsCarcinogens and Genotoxicity Assessment

The DOI matches its Crossref record; 123 of the 124 references it cites were found in a registry or an index.

Toxicological evaluation of proteins introduced into food crops

Open access
Hammond, Bruce, Kough, John, Herouet-Guicheney, Corinne, Jez, Joseph M., on behalf of the ILSI International Food Biotechnology Committee Task Force on the Use of Mammalian Toxicology Studies in the Safety Assessment of GM Foods·2013·Critical Reviews in Toxicology
DOI 10.3109/10408444.2013.842956PMC PMC3835160
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Abstract

This manuscript focuses on the toxicological evaluation of proteins introduced into GM crops to impart desired traits. In many cases, introduced proteins can be shown to have a history of safe use. Where modifications have been made to proteins, experience has shown that it is highly unlikely that modification of amino acid sequences can make a non-toxic protein toxic. Moreover, if the modified protein still retains its biological function, and this function is found in related proteins that have a history of safe use (HOSU) in food, and the exposure level is similar to functionally related proteins, then the modified protein could also be considered to be "as-safe-as" those that have a HOSU. Within nature, there can be considerable evolutionary changes in the amino acid sequence of proteins within the same family, yet these proteins share the same biological function. In general, food crops such as maize, soy, rice, canola etc. are subjected to a variety of processing conditions to generate different food products. Processing conditions such as cooking, modification of pH conditions, and mechanical shearing can often denature proteins in these crops resulting in a loss of functional activity. These same processing conditions can also markedly lower human dietary exposure to (functionally active) proteins. Safety testing of an introduced protein could be indicated if its biological function was not adequately characterized and/or it was shown to be structurally/functionally related to proteins that are known to be toxic to mammals.

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Figures

Figure 1. Comparison of three-dimensional structures of EPSPS from plants and bacteria. The X-ray crystal structures of the EPSPS from E. coli and Agrobacterium CP4 were used to generate homology models of the EPSPS from canola, maize, rice, and soy using SwissModel. The plant enzymes have ∼90% sequence identity with each other and are ∼50% identical to the bacterial enzymes. Secondary structure corresponding to α-helices and β-strands are colored blue and gold, respectively. The position of glyphosate (from the E. coli and CP4 crystal structures) is modeled as a space-filling molecule (red) into each structure to show the active site location.
Figure 1. Comparison of three-dimensional structures of EPSPS from plants and bacteria. The X-ray crystal structures of the EPSPS from E. coli and Agrobacterium CP4 were used to generate homology models of the EPSPS from canola, maize, rice, and soy using SwissModel. The plant enzymes have ∼90% sequence identity with each other and are ∼50% identical to the bacterial enzymes. Secondary structure corresponding to α-helices and β-strands are colored blue and gold, respectively. The position of glyphosate (from the E. coli and CP4 crystal structures) is modeled as a space-filling molecule (red) into each structure to show the active site location.CC BY-NC · PubMed Central
Figure 2. Cytochrome c oxidase structural homology. Comparison of the three-dimensional structures and active sites of cytochrome c oxidases from various species. Overall structure is shown as a ribbon diagram. Invariant residues (gold spheres) that maintain the position of the catalytic heme-group (rose spheres) are highlighted.
Figure 2. Cytochrome c oxidase structural homology. Comparison of the three-dimensional structures and active sites of cytochrome c oxidases from various species. Overall structure is shown as a ribbon diagram. Invariant residues (gold spheres) that maintain the position of the catalytic heme-group (rose spheres) are highlighted.CC BY-NC · PubMed Central
Figure 3. Variety of protein structures. Examples of different types of proteins are shown to highlight variations in secondary, tertiary, and quaternary structures. In panel A, the gold space-filling model represents DNA and the green ribbon diagram the protein. In panel B, each subunit of the proteasome is colored differently. In panel C, the monomeric structure of porin is shown as a ribbon diagram. In panel D, the viral peptide is shown as the brown space-filling model and the major histocompatibility complex (MHC) molecule as a ribbon diagram.
Figure 3. Variety of protein structures. Examples of different types of proteins are shown to highlight variations in secondary, tertiary, and quaternary structures. In panel A, the gold space-filling model represents DNA and the green ribbon diagram the protein. In panel B, each subunit of the proteasome is colored differently. In panel C, the monomeric structure of porin is shown as a ribbon diagram. In panel D, the viral peptide is shown as the brown space-filling model and the major histocompatibility complex (MHC) molecule as a ribbon diagram.CC BY-NC · PubMed Central

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Citations

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Research works printed but not linked: 22

  1. Concon JM, 1988, Food toxicology, part a. principles and concepts, 405
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  14. EFSA, 2010, EFSA J, 8, 1564
  15. Hammond B, 2008, Food Safety of Proteins in Agricultural Biotechnology, 259
  16. ILSI, 2007, Sampling and Detection Methods for Products of Modern Agricultural Biotechnology in NAFTA Countries. ILSI International Food Biotechnology Committee (IFBiC) Workshop, October 11–12, 2007
  17. IPCS (International Programme on Chemical Safety), 1999, Environmental Health Criteria, 217, Microbial Pest Control Agent Bacillus thuringiensis
  18. O’Hagan DT, 1988, Crit Rev Ther Drug Carrier Syst, 4, 197
  19. Pearce RJ, 1989, Bull Int Dairy Fed, 238, 17
  20. Pyler EJ, 2009, Baking science & technology Vol. II: formulation and production
  21. US EPA, 2009, Position Paper on Scientific Issues Associated with the Data Required to Register Plant-Incorporated Protectants
  22. US EPA, 2010, Biopesticides Registration Action Document: Modified Cry3A Protein and the Genetic Material Necessary for its Production (Via Elements of pZM26) in Event MIR604 Corn SYN-IR604–8

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Metadata

Authors
Hammond, B., Kough, J., Herouet-Guicheney, C., Jez, J. M., & on behalf of the ILSI International Food Biotechnology Committee Task Force on the Use of Mammalian Toxicology Studies in the Safety Assessment of GM Foods
Affiliations
  • Monsanto (United States) (US)
  • Environmental Protection Agency (US)
  • Washington University in St. Louis (US)
Corresponding author
Hammond, Bruce
ORCID
Jez, Joseph M.
Venue
Critical Reviews in Toxicology
Publisher
Informa UK Limited
Published
2013-10-28
Volume
43
Issue
sup2
Pages
25-42
ISSN
  • 0045-6446 (ISSN-L)
  • 1040-8444
  • 1547-6898
DOI
10.3109/10408444.2013.842956
PMC
PMC3835160
OpenAlex
W2101621051
Cited by
110
References
124
Citations by year
2026: 4 · 2025: 9 · 2024: 4 · 2023: 3 · 2022: 8 · 2021: 7 · 2020: 8 · 2019: 16 · 2018: 13 · 2017: 11 · 2016: 13 · 2015: 9 · 2014: 5
FWCI
0.96
Type
journal article
Language
en
Open access
Locations
  • Critical Reviews in Toxicology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
  • PepsiCo
  • Daegu Haany University
  • Universität Wien
  • Chinese Center for Disease Control and Prevention
  • Medizinische Universität Wien
  • Novus International
  • University of Illinois at Urbana-Champaign
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Genetically Modified Organisms Research
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Agricultural safety and regulations
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Carcinogens and Genotoxicity Assessment
Keywords
genetically modified crops, food safety, protein modification, protein denaturation, food processing, dietary exposure, toxicological evaluation
MeSH terms
Amino Acid Sequence, Animals, Humans, Plant Proteins, Proteins, Risk Assessment, Toxicity Tests, Plants, Genetically Modified, Food, Genetically Modified, Food Safety

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