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Dietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease.

Frontiers in nutrition

Zheng J, Wang M, Wei W, Keller JN, Adhikari B, King JF, King ML, Peng N, Laine RA.
PMID: 27014695
Front Nutr. 2016 Mar 07;3:7. doi: 10.3389/fnut.2016.00007. eCollection 2016.

Lectins from dietary plants have been shown to enhance drug absorption in the gastrointestinal tract of rats, be transported trans-synaptically as shown by tracing of axonal and dendritic paths, and enhance gene delivery. Other carbohydrate-binding protein toxins are known...

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Zheng J, Wang M, Wei W, et al. Dietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease. Front Nutr. 2016;3:7doi: 10.3389/fnut.2016.00007.
Zheng, J., Wang, M., Wei, W., Keller, J. N., Adhikari, B., King, J. F., King, M. L., Peng, N., & Laine, R. A. (2016). Dietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease. Frontiers in nutrition, 37. https://doi.org/10.3389/fnut.2016.00007
Zheng, Jolene, et al. "Dietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease." Frontiers in nutrition vol. 3 (2016): 7. doi: https://doi.org/10.3389/fnut.2016.00007
Zheng J, Wang M, Wei W, Keller JN, Adhikari B, King JF, King ML, Peng N, Laine RA. Dietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease. Front Nutr. 2016 Mar 07;3:7. doi: 10.3389/fnut.2016.00007. eCollection 2016. PMID: 27014695; PMCID: PMC4780318.
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Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola.

Science (New York, N.Y.)

Kozloff LM, Lute M, Westaway D.
PMID: 17759892
Science. 1984 Nov 16;226(4676):845-6. doi: 10.1126/science.226.4676.845.

Phosphatidylinositol has been identified as a major component of the ice nucleating site on the outer surface of two bacteria, Pseudomonas syringae and Erwinia herbicola. Plant lectins binding to inositol and a highly purified phosphatidylinositol-specific hydrolase (a C(II) lipase)...

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Kozloff LM, Lute M, Westaway D. Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science. 1984;226(4676):845-6doi: 10.1126/science.226.4676.845.
Kozloff, L. M., Lute, M., & Westaway, D. (1984). Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science (New York, N.Y.), 226(4676), 845-6. https://doi.org/10.1126/science.226.4676.845
Kozloff, L M, et al. "Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola." Science (New York, N.Y.) vol. 226,4676 (1984): 845-6. doi: https://doi.org/10.1126/science.226.4676.845
Kozloff LM, Lute M, Westaway D. Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science. 1984 Nov 16;226(4676):845-6. doi: 10.1126/science.226.4676.845. PMID: 17759892.
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Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L.

Plant physiology

Pueppke SG.
PMID: 16661012
Plant Physiol. 1979 Oct;64(4):575-80. doi: 10.1104/pp.64.4.575.

Peanut lectin was purified from seed meal of the Spanish and Jumbo Virginia varieties of peanut (Arachis hypogaea L.) by affinity chromatography on lactose coupled to Sepharose 4B. Polyacrylamide gel isoelectric focusing resolved the lectin preparation from Jumbo Virginia...

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Pueppke SG. Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L. Plant Physiol. 1979;64(4):575-80doi: 10.1104/pp.64.4.575.
Pueppke, S. G. (1979). Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L. Plant physiology, 64(4), 575-80. https://doi.org/10.1104/pp.64.4.575
Pueppke, S G. "Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L." Plant physiology vol. 64,4 (1979): 575-80. doi: https://doi.org/10.1104/pp.64.4.575
Pueppke SG. Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L. Plant Physiol. 1979 Oct;64(4):575-80. doi: 10.1104/pp.64.4.575. PMID: 16661012; PMCID: PMC543140.
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Antiviral agents targeting glycans on dengue virus E-glycoprotein.

Expert review of anti-infective therapy

Hidari KI, Suzuki T.
PMID: 22029517
Expert Rev Anti Infect Ther. 2011 Nov;9(11):983-5. doi: 10.1586/eri.11.115.

The molecular recognition of dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) with arthropod-derived N-glycans on E-glycoprotein is essential for dengue virus (DENV) infection in humans. Therefore, the specific interaction of DC-SIGN with N-glycans on E-glycoprotein is a promising...

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Hidari KI, Suzuki T. Antiviral agents targeting glycans on dengue virus E-glycoprotein. Expert Rev Anti Infect Ther. 2011;9(11):983-5doi: 10.1586/eri.11.115.
Hidari, K. I., & Suzuki, T. (2011). Antiviral agents targeting glycans on dengue virus E-glycoprotein. Expert review of anti-infective therapy, 9(11), 983-5. https://doi.org/10.1586/eri.11.115
Hidari, Kazuya I P J, and Suzuki, Takashi. "Antiviral agents targeting glycans on dengue virus E-glycoprotein." Expert review of anti-infective therapy vol. 9,11 (2011): 983-5. doi: https://doi.org/10.1586/eri.11.115
Hidari KI, Suzuki T. Antiviral agents targeting glycans on dengue virus E-glycoprotein. Expert Rev Anti Infect Ther. 2011 Nov;9(11):983-5. doi: 10.1586/eri.11.115. PMID: 22029517.
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Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs).

Bioinformation

Archak S, Nagaraju J.
PMID: 24616556
Bioinformation. 2014 Feb 19;10(2):63-7. doi: 10.6026/97320630010063. eCollection 2014.

Eicosapenta peptide repeats (EPRs) occur exclusively in flowering plant genomes and exhibit very high amino acid residue conservation across occurrence. DNA and amino acid sequence searches yielded no indications about the function due to absence of similarity to known...

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Archak S, Nagaraju J. Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs). Bioinformation. 2014;10(2):63-7doi: 10.6026/97320630010063.
Archak, S., & Nagaraju, J. (2014). Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs). Bioinformation, 10(2), 63-7. https://doi.org/10.6026/97320630010063
Archak, Sunil, and Nagaraju, Javaregowda. "Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs)." Bioinformation vol. 10,2 (2014): 63-7. doi: https://doi.org/10.6026/97320630010063
Archak S, Nagaraju J. Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs). Bioinformation. 2014 Feb 19;10(2):63-7. doi: 10.6026/97320630010063. eCollection 2014. PMID: 24616556; PMCID: PMC3937577.
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Lectin domains at the frontiers of plant defense.

Frontiers in plant science

Lannoo N, Van Damme EJ.
PMID: 25165467
Front Plant Sci. 2014 Aug 13;5:397. doi: 10.3389/fpls.2014.00397. eCollection 2014.

Plants are under constant attack from pathogens and herbivorous insects. To protect and defend themselves, plants evolved a multi-layered surveillance system, known as the innate immune system. Plants sense their encounters upon perception of conserved microbial structures and damage-associated...

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Lannoo N, Van Damme EJ. Lectin domains at the frontiers of plant defense. Front Plant Sci. 2014;5:397doi: 10.3389/fpls.2014.00397.
Lannoo, N., & Van Damme, E. J. (2014). Lectin domains at the frontiers of plant defense. Frontiers in plant science, 5397. https://doi.org/10.3389/fpls.2014.00397
Lannoo, Nausicaä, and Van Damme, Els J M. "Lectin domains at the frontiers of plant defense." Frontiers in plant science vol. 5 (2014): 397. doi: https://doi.org/10.3389/fpls.2014.00397
Lannoo N, Van Damme EJ. Lectin domains at the frontiers of plant defense. Front Plant Sci. 2014 Aug 13;5:397. doi: 10.3389/fpls.2014.00397. eCollection 2014. PMID: 25165467; PMCID: PMC4131498.
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Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study.

Frontiers in plant science

Oliveira C, Teixeira JA, Domingues L.
PMID: 25152749
Front Plant Sci. 2014 Aug 08;5:390. doi: 10.3389/fpls.2014.00390. eCollection 2014.

Frutalin is a homotetrameric partly glycosylated α-D-galactose-binding lectin of biomedical interest from Artocarpus incisa (breadfruit) seeds, belonging to the jacalin-related lectins family. As other plant lectins, frutalin is a heterogeneous mixture of several isoforms possibly with distinct biological activities....

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Oliveira C, Teixeira JA, Domingues L. Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study. Front Plant Sci. 2014;5:390doi: 10.3389/fpls.2014.00390.
Oliveira, C., Teixeira, J. A., & Domingues, L. (2014). Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study. Frontiers in plant science, 5390. https://doi.org/10.3389/fpls.2014.00390
Oliveira, Carla, et al. "Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study." Frontiers in plant science vol. 5 (2014): 390. doi: https://doi.org/10.3389/fpls.2014.00390
Oliveira C, Teixeira JA, Domingues L. Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study. Front Plant Sci. 2014 Aug 08;5:390. doi: 10.3389/fpls.2014.00390. eCollection 2014. PMID: 25152749; PMCID: PMC4126444.
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Fluorescent Neoglycoprotein Gold Nanoclusters: Synthesis and Applications in Plant Lectin Sensing and Cell Imaging.

Nanoscale research letters

Brzezicka KA, Serna S, Reichardt NC.
PMID: 30421263
Nanoscale Res Lett. 2018 Nov 12;13(1):360. doi: 10.1186/s11671-018-2772-2.

Carbohydrate-protein interactions mediate fundamental biological processes, such as fertilization, cell signaling, or host-pathogen communication. However, because of the enormous complexity of glycan recognition events, new tools enabling their analysis or applications emerge in recent years. Here, we describe the...

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Brzezicka KA, Serna S, Reichardt NC. Fluorescent Neoglycoprotein Gold Nanoclusters: Synthesis and Applications in Plant Lectin Sensing and Cell Imaging. Nanoscale Res Lett. 2018;13(1):360doi: 10.1186/s11671-018-2772-2.
Brzezicka, K. A., Serna, S., & Reichardt, N. C. (2018). Fluorescent Neoglycoprotein Gold Nanoclusters: Synthesis and Applications in Plant Lectin Sensing and Cell Imaging. Nanoscale research letters, 13(1), 360. https://doi.org/10.1186/s11671-018-2772-2
Brzezicka, Katarzyna Alicja, et al. "Fluorescent Neoglycoprotein Gold Nanoclusters: Synthesis and Applications in Plant Lectin Sensing and Cell Imaging." Nanoscale research letters vol. 13,1 (2018): 360. doi: https://doi.org/10.1186/s11671-018-2772-2
Brzezicka KA, Serna S, Reichardt NC. Fluorescent Neoglycoprotein Gold Nanoclusters: Synthesis and Applications in Plant Lectin Sensing and Cell Imaging. Nanoscale Res Lett. 2018 Nov 12;13(1):360. doi: 10.1186/s11671-018-2772-2. PMID: 30421263; PMCID: PMC6232188.
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Messages From the Past: New Insights in Plant Lectin Evolution.

Frontiers in plant science

Van Holle S, Van Damme EJM.
PMID: 30761173
Front Plant Sci. 2019 Jan 29;10:36. doi: 10.3389/fpls.2019.00036. eCollection 2019.

Lectins are a large and diverse class of proteins, found in all kingdoms of life. Plants are known to express different types of carbohydrate-binding proteins, each containing at least one particular lectin domain which enables them to specifically recognize...

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Van Holle S, Van Damme EJM. Messages From the Past: New Insights in Plant Lectin Evolution. Front Plant Sci. 2019;10:36doi: 10.3389/fpls.2019.00036.
Van Holle, S., & Van Damme, E. J. M. (2019). Messages From the Past: New Insights in Plant Lectin Evolution. Frontiers in plant science, 1036. https://doi.org/10.3389/fpls.2019.00036
Van Holle, Sofie, and Van Damme, Els J M. "Messages From the Past: New Insights in Plant Lectin Evolution." Frontiers in plant science vol. 10 (2019): 36. doi: https://doi.org/10.3389/fpls.2019.00036
Van Holle S, Van Damme EJM. Messages From the Past: New Insights in Plant Lectin Evolution. Front Plant Sci. 2019 Jan 29;10:36. doi: 10.3389/fpls.2019.00036. eCollection 2019. PMID: 30761173; PMCID: PMC6362431.
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Combining Click Reactions for the One-Pot Synthesis of Modular Biomolecule Mimetics.

Organic letters

Brinkø A, Risinger C, Lambert A, Blixt O, Grandjean C, Jensen HH.
PMID: 31502847
Org Lett. 2019 Sep 20;21(18):7544-7548. doi: 10.1021/acs.orglett.9b02811. Epub 2019 Sep 10.

Here, we report on the first combined one-pot use of the two so-called "click reactions": the thiol-ene coupling and the copper-catalyzed alkyne-azide cycloaddition. These reactions were employed in an alternating and one-pot fashion to combine appropriately functionalized monomeric carbohydrate...

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Brinkø A, Risinger C, Lambert A, et al. Combining Click Reactions for the One-Pot Synthesis of Modular Biomolecule Mimetics. Org Lett. 2019;21(18):7544-7548doi: 10.1021/acs.orglett.9b02811.
Brinkø, A., Risinger, C., Lambert, A., Blixt, O., Grandjean, C., & Jensen, H. H. (2019). Combining Click Reactions for the One-Pot Synthesis of Modular Biomolecule Mimetics. Organic letters, 21(18), 7544-7548. https://doi.org/10.1021/acs.orglett.9b02811
Brinkø, Anne, et al. "Combining Click Reactions for the One-Pot Synthesis of Modular Biomolecule Mimetics." Organic letters vol. 21,18 (2019): 7544-7548. doi: https://doi.org/10.1021/acs.orglett.9b02811
Brinkø A, Risinger C, Lambert A, Blixt O, Grandjean C, Jensen HH. Combining Click Reactions for the One-Pot Synthesis of Modular Biomolecule Mimetics. Org Lett. 2019 Sep 20;21(18):7544-7548. doi: 10.1021/acs.orglett.9b02811. Epub 2019 Sep 10. PMID: 31502847.
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Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

Ahmed MN, Jahan R, Nissapatorn V, Wilairatana P, Rahmatullah M.
PMID: 34891122
Biomed Pharmacother. 2021 Dec 07;146:112507. doi: 10.1016/j.biopha.2021.112507. Epub 2021 Dec 07.

Lectins or clusters of carbohydrate-binding proteins of non-immune origin are distributed chiefly in the Plantae. Lectins have potent anti-infectivity properties for several RNA viruses including SARS-CoV-2. The primary purpose of this review is to review the ability of lectins...

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Ahmed MN, Jahan R, Nissapatorn V, et al. Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies. Biomed Pharmacother. 2021;146:112507doi: 10.1016/j.biopha.2021.112507.
Ahmed, M. N., Jahan, R., Nissapatorn, V., Wilairatana, P., & Rahmatullah, M. (2021). Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 146112507. https://doi.org/10.1016/j.biopha.2021.112507
Ahmed, Md Nasir, et al. "Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies." Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie vol. 146 (2021): 112507. doi: https://doi.org/10.1016/j.biopha.2021.112507
Ahmed MN, Jahan R, Nissapatorn V, Wilairatana P, Rahmatullah M. Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies. Biomed Pharmacother. 2021 Dec 07;146:112507. doi: 10.1016/j.biopha.2021.112507. Epub 2021 Dec 07. PMID: 34891122; PMCID: PMC8648558.
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Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils.

International journal of biological macromolecules

Grigorieva DV, Gorudko IV, Grudinina NA, Panasenko OM, Semak IV, Sokolov AV, Timoshenko AV.
PMID: 34863835
Int J Biol Macromol. 2021 Dec 01;195:30-40. doi: 10.1016/j.ijbiomac.2021.11.165. Epub 2021 Dec 01.

Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficiently modified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammation and oxidative/halogenative stress by myeloperoxidase, an enzyme of...

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Grigorieva DV, Gorudko IV, Grudinina NA, et al. Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils. Int J Biol Macromol. 2021;195:30-40doi: 10.1016/j.ijbiomac.2021.11.165.
Grigorieva, D. V., Gorudko, I. V., Grudinina, N. A., Panasenko, O. M., Semak, I. V., Sokolov, A. V., & Timoshenko, A. V. (2021). Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils. International journal of biological macromolecules, 19530-40. https://doi.org/10.1016/j.ijbiomac.2021.11.165
Grigorieva, Daria V, et al. "Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils." International journal of biological macromolecules vol. 195 (2021): 30-40. doi: https://doi.org/10.1016/j.ijbiomac.2021.11.165
Grigorieva DV, Gorudko IV, Grudinina NA, Panasenko OM, Semak IV, Sokolov AV, Timoshenko AV. Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils. Int J Biol Macromol. 2021 Dec 01;195:30-40. doi: 10.1016/j.ijbiomac.2021.11.165. Epub 2021 Dec 01. PMID: 34863835.
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