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Article ; Online: Double-Mutated 5-Enol Pyruvylshikimate-3-phosphate Synthase Protein Expressed in MZHG0JG Corn (Zea mays L.) Has No Impact on Toxicological Safety and Nutritional Composition.

Matthews, Bethany A / Launis, Karen L / Bauman, Patricia A / Juba, Nicole C

Journal of agricultural and food chemistry

2017 Volume 65, Issue 38, Page(s) 8459–8465

Abstract: MZHG0JG corn will offer growers the flexibility to alternate between herbicides with two different modes of action in their weed-management programs, helping to mitigate and manage the evolution of herbicide resistance in weed populations. The proteins ... ...

Abstract	MZHG0JG corn will offer growers the flexibility to alternate between herbicides with two different modes of action in their weed-management programs, helping to mitigate and manage the evolution of herbicide resistance in weed populations. The proteins conferring herbicide tolerence in MZHG0JG corn, double-mutated 5-enol pyruvylshikimate-3-phosphate synthase protein (mEPSPS) and phosphinothricin acetyltransferase (PAT), as well as the MZHG0JG corn event, have been assessed by regulatory authorities globally and have been determined to be safe for humans, animals, and the environment. In addition to the safety data available for these proteins, further studies were conducted on MZHG0JG corn to assess levels of mEPSPS as compared to previously registered genetically modified (GM) corn. The results support the conclusion of no impact on toxicological safety or nutritional composition.
Language	English
Publishing date	2017-09-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.7b02217
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Article ; Online: "From Protein Toxins to Applied Toxicological Testing" virtual workshop identifies the need for a bioinformatic framework to assess novel food protein safety.

Bauman, Patricia A / Doxey, Andrew C / Eberini, Ivano / Islamovic, Emir / Jungo, Florence / Kessenich, Colton / Kough, John / Krishan, Mansi / Palazzolo, Luca / Privalle, Laura / Rodriguez, Chester E / Satchell, Karla J F / Silvanovich, Andre / Pereira Mouriès, Lucilia

Regulatory toxicology and pharmacology : RTP

2022 Volume 131, Page(s) 105146

Abstract: On October 21-22, 2020 the HESI (Health and Environmental Sciences Institute) Protein Allergens, Toxins, and Bioinformatics Committee, and the Society of Toxicology Food Safety Specialty Section co-hosted a virtual workshop titled "From Protein Toxins to ...

Abstract	On October 21-22, 2020 the HESI (Health and Environmental Sciences Institute) Protein Allergens, Toxins, and Bioinformatics Committee, and the Society of Toxicology Food Safety Specialty Section co-hosted a virtual workshop titled "From Protein Toxins to Applied Toxicological Testing". The workshop focused on the safety assessment of novel proteins contained in foods and feeds, was globally represented by over 200 stakeholder attendees, and featured contributions from experts in academia, government and non-government organizations, and agricultural biotechnology developers from the private sector. A range of topics relevant to novel protein safety were discussed, including: the state of protein toxin biology, modes and mechanisms of action, structures and activity, use of bioinformatic analyses to assess the safety of a protein, and ways to leverage computational biology with in silico approaches for protein toxin identification/characterization. Key outcomes of the workshop included the appreciation of the complexity of developing a definition for a protein toxin when viewed from the perspective of food and feed safety, confirming the need for a case-by-case hypothesis-driven interpretation of bioinformatic results that leverages additional metadata rather than an alignment threshold-driven interpretation, and agreement that a "toxin protein database" is not necessary, as the bioinformatic needs for toxin detection may be accomplished by existing databases such as Pfam and UniProtKB/Swiss-Prot. In this paper, a path forward is proposed.
MeSH term(s)	Allergens/chemistry ; Allergens/toxicity ; Biotechnology/methods ; Computational Biology ; Databases, Protein ; Food Safety
Chemical Substances	Allergens
Language	English
Publishing date	2022-02-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	604672-1
ISSN	1096-0295 ; 0273-2300
ISSN (online)	1096-0295
ISSN	0273-2300
DOI	10.1016/j.yrtph.2022.105146
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Article: Double-Mutated 5-Enol Pyruvylshikimate-3-phosphate Synthase Protein Expressed in MZHG0JG Corn (Zea mays L.) Has No Impact on Toxicological Safety and Nutritional Composition

Matthews, Bethany A / Launis Karen L / Bauman Patricia A / Juba Nicole C

Journal of agricultural and food chemistry. 2017 Sept. 27, v. 65, no. 38

2017

Abstract	MZHG0JG corn will offer growers the flexibility to alternate between herbicides with two different modes of action in their weed-management programs, helping to mitigate and manage the evolution of herbicide resistance in weed populations. The proteins conferring herbicide tolerence in MZHG0JG corn, double-mutated 5-enol pyruvylshikimate-3-phosphate synthase protein (mEPSPS) and phosphinothricin acetyltransferase (PAT), as well as the MZHG0JG corn event, have been assessed by regulatory authorities globally and have been determined to be safe for humans, animals, and the environment. In addition to the safety data available for these proteins, further studies were conducted on MZHG0JG corn to assess levels of mEPSPS as compared to previously registered genetically modified (GM) corn. The results support the conclusion of no impact on toxicological safety or nutritional composition.
Keywords	Zea mays ; corn ; evolution ; growers ; herbicide resistance ; herbicides ; humans ; mechanism of action ; nutrient content ; phosphinothricin acetyltransferase ; proteins ; transgenic plants ; weeds
Language	English
Dates of publication	2017-0927
Size	p. 8459-8465.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021%2Facs.jafc.7b02217
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Article: Mass spectrometric analysis of digesta does not improve the allergenicity assessment of GM crops

Herman, Rod A / Bauman, Patricia A / Goodwin, Laurie / Islamovic, Emir / Ma, Eric H / Serrano, Hector / Silvanovich, Andre / Simmons, Abigail R / Song, Ping / Tetteh, Afua O / Wang, Rong

Transgenic research. 2021 June, v. 30, no. 3

2021

Abstract: An investigation of the potential allergenicity of newly expressed proteins in genetically modified (GM) crops comprises part of the assessment of GM crop safety. However, allergenicity is not completely predictable from a definitive assay result or set ... ...

Abstract	An investigation of the potential allergenicity of newly expressed proteins in genetically modified (GM) crops comprises part of the assessment of GM crop safety. However, allergenicity is not completely predictable from a definitive assay result or set of protein characteristics, and scientific opinions regarding the data that should be used to assess allergenicity are continuously evolving. Early studies supported a correlation between the stability of a protein exposed to digestive enzymes such as pepsin and the protein’s status as a potential allergen, but over time the conclusions of these earlier studies were not confirmed. Nonetheless, many regulatory authorities, including the European Food Safety Authority (EFSA), continue to require digestibility analyses as a component of GM crop risk assessments. Moreover, EFSA has recently investigated the use of mass spectrometry (MS), to make digestion assays more predictive of allergy risk, because it can detect and identify small undigested peptides. However, the utility of MS is questionable in this context, since known allergenic peptides are unlikely to exist in protein candidates intended for commercial development. These protein candidates are pre-screened by the same bioinformatics processes that are normally used to identify MS targets. Therefore, MS is not a standalone allergen identification method and also cannot be used to predict previously unknown allergenic epitopes. Thus, the suggested application of MS for analysis of digesta does not improve the poor predictive power of digestion assays in identifying allergenic risk.
Keywords	allergenicity ; allergens ; bioinformatics ; crop safety ; digesta ; digestibility ; digestion ; epitopes ; food safety ; genetic engineering ; hypersensitivity ; mass spectrometry ; pepsin ; peptides ; risk
Language	English
Dates of publication	2021-06
Size	p. 283-288.
Publishing place	Springer International Publishing
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	31620-9
ISSN	1573-9368 ; 0962-8819
ISSN (online)	1573-9368
ISSN	0962-8819
DOI	10.1007/s11248-021-00254-x
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Article ; Online: Mass spectrometric analysis of digesta does not improve the allergenicity assessment of GM crops.

Herman, Rod A / Bauman, Patricia A / Goodwin, Laurie / Islamovic, Emir / Ma, Eric H / Serrano, Hector / Silvanovich, Andre / Simmons, Abigail R / Song, Ping / Tetteh, Afua O / Wang, Rong

Transgenic research

2021 Volume 30, Issue 3, Page(s) 283–288

Abstract	An investigation of the potential allergenicity of newly expressed proteins in genetically modified (GM) crops comprises part of the assessment of GM crop safety. However, allergenicity is not completely predictable from a definitive assay result or set of protein characteristics, and scientific opinions regarding the data that should be used to assess allergenicity are continuously evolving. Early studies supported a correlation between the stability of a protein exposed to digestive enzymes such as pepsin and the protein's status as a potential allergen, but over time the conclusions of these earlier studies were not confirmed. Nonetheless, many regulatory authorities, including the European Food Safety Authority (EFSA), continue to require digestibility analyses as a component of GM crop risk assessments. Moreover, EFSA has recently investigated the use of mass spectrometry (MS), to make digestion assays more predictive of allergy risk, because it can detect and identify small undigested peptides. However, the utility of MS is questionable in this context, since known allergenic peptides are unlikely to exist in protein candidates intended for commercial development. These protein candidates are pre-screened by the same bioinformatics processes that are normally used to identify MS targets. Therefore, MS is not a standalone allergen identification method and also cannot be used to predict previously unknown allergenic epitopes. Thus, the suggested application of MS for analysis of digesta does not improve the poor predictive power of digestion assays in identifying allergenic risk.
MeSH term(s)	Allergens/adverse effects ; Allergens/immunology ; Allergens/isolation & purification ; Crops, Agricultural/adverse effects ; Crops, Agricultural/chemistry ; Crops, Agricultural/immunology ; Food Safety ; Food, Genetically Modified/adverse effects ; Humans ; Mass Spectrometry ; Plants, Genetically Modified/adverse effects ; Plants, Genetically Modified/chemistry ; Plants, Genetically Modified/immunology
Chemical Substances	Allergens
Language	English
Publishing date	2021-04-16
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	31620-9
ISSN	1573-9368 ; 0962-8819
ISSN (online)	1573-9368
ISSN	0962-8819
DOI	10.1007/s11248-021-00254-x
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Article: Determinants within the C-terminus of the human norepinephrine transporter dictate transporter trafficking, stability, and activity.

Bauman, Patricia A / Blakely, Randy D

Archives of biochemistry and biophysics

2002 Volume 404, Issue 1, Page(s) 80–91

Abstract: The function of the human norepinephrine transporter (hNET) depends on its presence at the cell surface. A role for the hNET C-terminus in trafficking the transporter to the surface has been suggested by the report of a bovine NET C-terminal splice ... ...

Abstract	The function of the human norepinephrine transporter (hNET) depends on its presence at the cell surface. A role for the hNET C-terminus in trafficking the transporter to the surface has been suggested by the report of a bovine NET C-terminal splice variant that accumulates within heterologous host cells, and a human variant homolog has also been reported. We examined the relevance of the C-terminus of hNET to trafficking and function using transfected LLC-PK1 cells. The intracellular and surface expression of NET proteins was evaluated by Western blots, and their functional capacities were assessed using transport assays. We found that the C-terminal residues encoded by hNET 1a enable the efficient maturation and surface expression of hNET and therefore critically impact transporter activity. Alternative splicing causes the retention of immature hNETs within the cell, whereas introduced C-terminal deletions result in significant degradation. The loss of the terminal isoleucine alone (Delta617-hNET) is sufficient to cause the degradation of hNET, an effect that can be mimicked by nonconservative point mutations at the terminal position. The phenotype of Delta617-hNET is recapitulated in neuronal SK-N-MC cells, but is significantly less severe in HEK-293 cells, suggesting a role for host cell factors in enabling the biosynthetic progression of wild-type hNET. Additional proximal residues may act at other steps to affect the expression of the fully mature protein on the cell surface (Q608A) and to more directly affect transporter activity (F609A). Together our studies document a critical contribution of the hNET C-terminus to transporter trafficking, stability, and function.
MeSH term(s)	Alternative Splicing ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Biological Transport, Active ; Cell Membrane/metabolism ; Drug Stability ; Genetic Variation ; Humans ; LLC-PK1 Cells ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Norepinephrine Plasma Membrane Transport Proteins ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Deletion ; Swine ; Symporters/chemistry ; Symporters/genetics ; Symporters/metabolism ; Transfection
Chemical Substances	Norepinephrine Plasma Membrane Transport Proteins ; Peptide Fragments ; Recombinant Proteins ; SLC6A2 protein, human ; Symporters
Language	English
Publishing date	2002-06-25
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/s0003-9861(02)00232-1
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Article: Analysis of specific interactions of native protein phosphatase 1 isoforms with targeting subunits.

Colbran, Roger J / Carmody, Leigh C / Bauman, Patricia A / Wadzinski, Brian E / Bass, Martha A

Methods in enzymology

2003 Volume 366, Page(s) 156–175

Abstract: Expression of recombinant PP1 isoforms with fully authentic properties has proven to be a challenge for several laboratories. In order to circumvent this technical limitation in the investigation of isoform-specific roles for PP1, methods have been ... ...

Abstract	Expression of recombinant PP1 isoforms with fully authentic properties has proven to be a challenge for several laboratories. In order to circumvent this technical limitation in the investigation of isoform-specific roles for PP1, methods have been developed to analyze specific properties of native PP1 isoforms. The well-documented method of ethanol precipitation of tissue extracts has been used to dissociate phosphatase catalytic subunits from their endogenous regulatory subunits and other cellular proteins. Although very low levels of PP1 and PP2A regulatory subunits are sometimes detected in PPC preparations, they are not associated with their respective catalytic subunits because they do not copurify with the catalytic subunits on microcystin-Sepharose (Bauman & Colbran, not shown). Thus, the PPC preparation represents a mixture of native monomeric phosphatase catalytic subunits (including PP1 isoforms, PP2AC, PP4C, and PP6C) that can be used to analyze their interactions with other proteins. The methods described in this report rely on the availability of highly specific antibodies to PP1 isoforms. The sheep antibodies have previously proven effective for immunoblotting and immunoprecipitation, whereas rabbit antibodies have also been used for immunocytochemistry. This paper documents the use of these antibodies in Far-Western overlay and glutathione-agarose cosedimentation assays to investigate interactions of specific PP1 isoforms with recombinant fragments of PP1-targeting subunits (spinophilin, neurabin and GM). Moreover, covalent coupling of affinity-purified sheep antibodies to agarose provided a means for the immuno-isolation of PP1 beta and PP1 gamma 1 from the PPC preparation. Active catalytic subunits are recovered from the affinity resin using chaotropic agents, permitting for the first time the assessment of the effects of specific targeting subunits on activities of individual native PP1 isoforms. These methods have been used successfully to demonstrate that some PP1-interacting proteins discriminate among the isoforms. The isoform inhibition assays provide a measure of the binding equilibrium in the milieu of the phosphatase assay. For example, while some PP1-binding proteins inhibit native PP1 beta and native PP1 gamma 1 with equivalent potency (e.g., PKA-phosphorylated inhibitor-1), spinophilin, neurabin and GM differentiate between these two isoforms; spinophilin and neurabin fragments inhibit native PP1 gamma 1 approximately 20-fold more potently than they inhibit native PP1 beta (Fig. 4), whereas GM inhibits native PP1 beta more potently than native PP1 gamma 1 (not shown). Moreover, the activity of native PP1 gamma 1 is approximately 100-fold more sensitive to neurabin and spinophilin than is the activity of bacterially-expressed recombinant PP1 gamma 1 (Fig. 4). The interpretation of these inhibition assays is consistent with data obtained in Far-Western overlay (Fig. 2) and glutathione-agarose cosedimentation assays (Fig. 3), which assess more stable interactions of PP1 isoforms. Thus, spinophilin and neurabin selectively bind PP1 gamma 1 over PP1 beta, whereas GM is highly selective for PP1 beta. These data are consistent with previous experiments that showed spinophilin and neurabin are present in PP1 gamma 1 complexes in brain extracts, but not in PP1 beta complexes. Moreover, only PP1 beta has been identified in complexes with GM in muscle extracts, although these data did not exclude the possibility that other isoforms were also present. Presumably, these isoform-selective interactions confer different functions on PP1. In summary, we have developed methods that should prove useful in defining the isoform-selectivity of other PP1-targeting subunits. Moreover, these methods may be employed to identify domains in PP1-interacting proteins that confer isoform specificity. Similar strategies may also be used to explore interactions of protein phosphatase catalytic subunits with other proteins.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibody Specificity ; Brain/enzymology ; Isoenzymes/chemistry ; Isoenzymes/metabolism ; Kinetics ; Molecular Sequence Data ; Phosphoprotein Phosphatases/chemistry ; Phosphoprotein Phosphatases/genetics ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Prosencephalon/enzymology ; Protein Phosphatase 1 ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Rats ; Sequence Alignment ; Sequence Homology, Amino Acid
Chemical Substances	Isoenzymes ; Protein Subunits ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2003
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/s0076-6879(03)66014-3
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Article: A protein phosphatase-1gamma1 isoform selectivity determinant in dendritic spine-associated neurabin.

Carmody, Leigh C / Bauman, Patricia A / Bass, Martha A / Mavila, Nirmala / DePaoli-Roach, Anna A / Colbran, Roger J

The Journal of biological chemistry

2004 Volume 279, Issue 21, Page(s) 21714–21723

Abstract: Protein phosphatase-1 (PP1) catalytic subunit isoforms interact with diverse proteins, typically containing a canonical (R/K)(V/I)XF motif. Despite sharing approximately 90% amino acid sequence identity, PP1beta and PP1gamma1 have distinct subcellular ... ...

Abstract	Protein phosphatase-1 (PP1) catalytic subunit isoforms interact with diverse proteins, typically containing a canonical (R/K)(V/I)XF motif. Despite sharing approximately 90% amino acid sequence identity, PP1beta and PP1gamma1 have distinct subcellular localizations that may be determined by selective interactions with PP1-binding proteins. Immunoprecipitation studies from brain and muscle extracts demonstrated that PP1gamma1 selectively interacts with spinophilin and neurabin, F-actin-targeting proteins, whereas PP1beta selectively interacted with G(M)/R(GL), the striated-muscle glycogen-targeting subunit. Glutathione S-transferase (GST) fusion proteins containing residues 146-493 of neurabin (GST-Nb-(146-493)) or residues 1-240 of G(M)/R(GL) (GST-G(M)-(1-240)) recapitulated these isoform selectivities in binding and phosphatase activity inhibition assays. Site-directed mutagenesis indicated that this isoform selectivity was not due to sequence differences between the canonical PP1-binding motifs (neurabin, (457)KIKF(460); G(M)/R(GL), (65)RVSF(68)). A chimeric GST fusion protein containing residues 1-64 of G(M)/R(GL) fused to residues 457-493 of neurabin (GST-G(M)/Nb) selectively bound to and inhibited PP1gamma1, whereas a GST-Nb/G(M) chimera containing Nb-(146-460) fused to G(M)-(69-240) selectively interacted with and weakly inhibited PP1beta, implicating domain(s) C-terminal to the (R/K)(V/I)XF motif as determinants of PP1 isoform selectivity. Deletion of Pro(464) and Ile(465) in neurabin (deltaPI) to equally space a conserved cluster of amino acids from the (R/K)(V/I)XF motif as in G(M)/R(GL) severely compromised the ability of neurabin to bind and inhibit both isoforms but did not affect PP1gamma1 selectivity. Further analysis of a series of C-terminal truncated GST-Nb-(146-493) proteins identified residues 473-479 of neurabin as containing a crucial PP1gamma1-selectivity determinant. In combination, these data identify a novel PP1gamma1-selective interaction domain in neurabin that may allow for selective regulation and/or subcellular targeting of PP1 isoforms.
MeSH term(s)	Actins/chemistry ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Blotting, Western ; Brain/metabolism ; Catalytic Domain ; Dendrites/metabolism ; Dose-Response Relationship, Drug ; Gene Deletion ; Genetic Vectors ; Glutathione Transferase/metabolism ; Mice ; Microfilament Proteins/chemistry ; Molecular Sequence Data ; Muscles/metabolism ; Mutagenesis, Site-Directed ; Mutation ; Nerve Tissue Proteins/chemistry ; Phosphoprotein Phosphatases/chemistry ; Precipitin Tests ; Protein Binding ; Protein Isoforms ; Protein Phosphatase 1 ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/chemistry ; Sequence Homology, Amino Acid
Chemical Substances	Actins ; Microfilament Proteins ; Nerve Tissue Proteins ; Protein Isoforms ; Recombinant Fusion Proteins ; Recombinant Proteins ; neurabin ; Glutathione Transferase (EC 2.5.1.18) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2004-03-11
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M402261200
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