How to order if you are a Patient: Thank you for your interest in our testing. Since all our testing must be ordered by a licensed health care practitioner, please have your current healthcare provider contact us so we can set them up with a Vibrant account.
How to order if you are a Provider: If you are a current Vibrant client, please contact firstname.lastname@example.org or call your local Territory Sales Manager.
If you don’t have an account with Vibrant Wellness, please fill out a Client Application form to get started.
Measures IgG and IgA antibody response to lectins and aquaporins
The Vibrant Lectin Zoomer detects both IgA and IgG to lectins and aquaporins in the most comprehensive panel available.
The most comprehensive panel
- Vibrant evaluates sensitivity to 16 lectins and 7 aquaporins in the most frequently consumed and potentially problematic foods.
- A combined detection of both IgA and IgG reduces the possibility of missing reactivity.
- Identification of peptides instead of proteins reduces the possibility of cross-reactivity with similar species.
The most accurate results
- Vibrant is the only company that utilizes a fluorescent method of detecting food sensitivities on a silicon chip, while other labs use ELISA or other methods.
- Peptide-based microarray technique eliminates the requirement of testing different forms of lectin (raw vs. cooked) and removes the false positives caused by cross reaction with pollens often seen in raw extracts.
- Long mer peptides synthesized at high fidelity provide more specific antigen-antibody interactions.
The most effective clinical outcome
- Scale of reactivity may help make decisions between rotation or elimination diet.
- Early detection enables intervention by physicians to reduce the risk of development of autoimmunity.
Use Vibrant’s Lectin Zoomer to improve your understanding of unexplained symptoms associated with gastrointestinal, neurological, dermatological, or behavioral disorders.
Only healthcare providers licensed in their state may order laboratory testing.
- Lima bean
- Bell pepper
- Mung bean
- Kidney bean
- Bell pepper
Lectins are a large class of sugar-binding proteins that can be found in all forms of life. In plants, lectins are part of the natural defense against microorganisms, pests, and insects. Although lectin has been considered a low-level toxin, many members of the lectin protein family can agglutinate (clump together) and become problematic for human health.
The most common potentially toxic lectin-containing food groups are:
- Grains (especially wheat but also rice, oats, rye, barley, and corn)
- Legumes (all dried beans, including soy and peanuts)
- Nightshades (includes potato, tomato, eggplant, and pepper)
Major harmful effects of dietary lectins are:
- Resistant to digestion – they can overfeed certain species of gut bacteria that feed on lectins which may lead to gut dysbiosis
- Damage of gut epithelial lining – lectins may damage intestinal barrier cells or open up the tight junctions between the cells, increasing the development of intestinal permeability, which may increase risk for autoimmunity.
- Stimulation of immune system – lectins can provoke antibodies causing inflammatory immune responses.
Human immune systems can react to food lectins and produce IgG and IgA antibodies. Detection of these antibodies can help manage eating habits (in consultation with a dietitian or healthcare provider) and reduce the risk of development of more serious conditions.
Symptoms and conditions associated with Lectin and/or Aquaporin sensitivity:
- Intestinal permeability (“leaky gut syndrome”) (bloating, gas, and abdominal cramps)
- Rheumatoid arthritis (painful and swollen joints)
- Allergies (watery eyes, sniffling, sinus congestion, throat tightness, and itchy skin, mouth or tongue)
- Fatigue and tiredness
- Mental health problems (e.g., depression)
- Skin rashes (redness and itchiness)
- Hormonal fluctuations
- Frequent use of antibiotics
- Following vegan/vegetarian diet
- Family history of autoimmune disorders, especially rheumatoid arthritis
Aquaporins, also known as “water channels,” are integral membrane proteins that form pores in the membrane of biological cells to facilitate water transport between cells. Aquaporins are found in all cells and help move water through the cells in an organized manner. Aquaporin 4 (AQR-4) is the most prevalent aquaporin channel in the central nervous system. Aquaporins from food sources (e.g., spinach, soy, corn, tomato, etc.) show similarity to the brain AQR-4.
Because aquaporins from food are highly stable during food preparation and may enter the human body as intact proteins, they become antigenic and trigger the production of antibodies. The antibodies against food aquaporins can be cross-reactive to human AQR-4 and induce severe neuro autoimmune disorders.
Patient with antibodies to food aquaporins may benefit from a Vibrant Neural Zoomer test if neurological autoimmunity or cognitive decline are suspected.
In either case, antibodies to a food lectin or a food aquaporin are indicative of an immunological reaction and the food should be omitted from the patient’s diet.
What is a lectin and why should I test for them?
Lectins are a class of sugar-binding proteins that are largely present in plants. Evolutionarily, lectins serve as part of the defense mechanism of plants. They serve to “clump” or agglutinize. If a person is sensitive to a particular lectin, it can be problematic to human health because
1) Lectins are resistant to digestion and can overfeed certain species of gut bacteria leading to gut dysbiosis.
2) Many lectins have anti-nutrient effects and can damage the intestinal epithelial cells and open-up intestinal tight junctions, contributing to intestinal permeability.
3) Lectins can over-stimulate the immune system. If someone is sensitive to a particular food lectin, they will produce antibodies to that lectin which can cause an immune response and increase in inflammation.
What is an aquaporin and why should I test for them?
Aquaporins are “water channel” proteins that are found in cell wall membranes of many biological cells that help with the transport of water through the cell. Aquaporins are particularly concentrated in the central nervous system (CNS). Certain foods contain aquaporins that can have molecular mimicry with biological aquaporins and antibodies can cross react with CNS tissue. Thus, elevated antibodies to food aquaporins may be linked to neurological autoimmunity, inflammation, and associated symptoms.
Can I be positive for a particular food on the Vibrant Lectin Zoomer but negative for this Food on the Vibrant Food Sensitivity or vice versa?
Yes! Vibrant Food Sensitivity is measuring antibodies to whole food protein extracts. The Vibrant Lectin Zoomer tests antibodies specific to the lectin peptides within that food. Antigen/antibody binding is very specific, therefore, someone may produce antibodies to an entire food protein or only a single part of it (a peptide fragment in it).
- Peumans WJ, Van Damme EJ. Lectins as plant defense proteins. Plant Physiology. 1995; 109(2) : 347-352. Banwell JG, Howard R, Cooper D, Costerton JW. Intestinal microbial flora after feeding phytohemagglutinin lectins (Phaseolus vulgaris) to rats. Applied and Environmental Microbiology. 1985; 50(1) : 68-80.
- Vasconcelos IM, Oliveira JA. Antinutritional properties of plant lectins. Toxicon. 2004; 44(4): 385-403. Cordain L, Toohey L, Smith M, Hickey M. Modulation of immune function by dietary lectins in rheumatoid arthritis. British Journal of Nutrition. 2000; 83(3) : 207-217.
- Vaishnav R, Liu R, Chapman J, et al. Aquaporin-4 molecular mimicry and implication for neuromyelitis optics. Journal of Neuroimmunology. 2013; 260(1-2) : 92-98.
- Jarius S, Paul F, Franciotta D, et al. Mechanisms of disease: aquaporin-4 antibodies in neuromyelitis optica. Nature Clinical Practice Neurology. 2008; 4(4) : 202-214.
- Peumans WJ, Stinissen HM, Carlier AR. Isolation and partial characterization of wheat-ger-agglutinin-like lectins from rye (Secale cereal) and barley (Hordeum vulgare) embryos. Biochemical Journal. 1982; 203 : 239-243.
- Prodanov P, Atanasova N. An anti-B lectin from Zea mays everta. Folia Haematol Int Mag KlinMorpholBlutforsch. 1984;111(1):84-85.
- • Andersson U, Rosén L, Ostman E, et al. Metabolic effects of whole grain wheat and whole grain rye in the C57BL/6J mouse. Nutrition. 2010; 26(2) : 230-239.
- • Damon M, Zhang NZ, Haytowitz DB, Booth SL. Phylloquinone (vitamin K1) content of vegetables. Journal of Food Composition and Analysis. 2005; 18 : 751-758.
- Reddivari L., Hale AL, Miller JC. Determination of phenolic content, composition and their contribution to
- antioxidant activity in specialty potato selections. American Journal of Potato Research. 2007;84:275. Matsumoto I, Jimbo A, Mizuno Y. Purification and characterization of potato lectin. Journal of Biological Chemistry. 1983; 258(5) : 2886-2891.
- Carreno-Gómez B, Woodley JF, Florence AT. Studies on the uptake of tomato lectin nanoparticles in everted gut sacs. International Journal of Pharmaceutics. 1999; 183(1) : 7-11.
- Kolberg J, Michaelsen TE, Sletten K. Properties of a lectin from the seeds of Cicer arietinum. Hoppe-seyler’sZeitschrift fur physiologischeChemie. 1983; 264 : 655-664.
- Goldstein IJ, Poretz RD. The Lectins. Properties, Functions, and Applications in Biology and Medicine. Academic Press. 1986; 35-247.
- Chung IM, Yeo MA, Kim SJ, Moon HI. Protective effects of organic solvent fractions from the seeds of Vigna radiata L. wilczek against antioxidant mechanisms. Human & Experimental Toxicology. 2011;30(8) : 904-909. Hernández-Ramírez RU, Galván-Portillo MV, Ward MH, et al. Dietary intake of polyphenols, nitrate and nitrite and gastric cancer risk in Mexico City. International Journal of Cancer. 2009;125(6) : 1424-1430.
- Hu FB, Stampfer MJ. Nut consumption and risk of coronary heart disease: a review of epidemiologic evidence. Current Atherosclerosis Reports. 1999;1(3) : 204-209.
- Wang Q, Yu LG, Campbell BJ, et al. Indentification of intact peanut lectin in peripheral venous blood. Lancet.
- 1998;352(9143) : 1831-1832.
- Zhao Q, Duckworth CA, Wang W, et al. Peanut agglutinin appearance in the blood circulation after peanut ingestion mimics the action of endogenous galectin-3 to promote metastasis by interaction with cancer-associated MUC1. Carcinogenesis. 2014; 35(12) : 2815-2821.
- Hirose K, Imaeda N, Tokudome Y, et al. Soybean products and reduction of breast cancer risk: a case–control study in Japan. British Journal of Cancer. 2005; 93(1) : 15-22.
- Handbook of Foodborne Pathogenic Microorganisms and Natural Toxins. US Food and Drug Administration. Available at:https://www.fda.gov/downloads/Food/FoodborneIllnessContaminants/UCM297627.pdf Accessed January 2018.
- Vaishnav RA, Liu R, Chapman J, et al. Aquaporin 4 Molecular Mimicry and Implications for Neuromyelitis
- Optica. Journal of neuroimmunology. 2013;260(0):92-98.