Helix Plus


Edible snail compound supports healthy immune function


Helix aspersa (a species of edible snail similar to Helix pomatia) has a powerful lectin which helps the immune system to function more effectively and efficiently. This species of snail is not the common edible snail (‘escargot’), but rather a hard-to-identify distant relative.

Eat Right For Your Type brought attention to dietary lectins; however, the primary emphasis of the book was on negative effects of lectins, with a recommendation, in general, for their avoidance. But in the complex world we live in, where sometimes good is bad, and bad can be good, it should come as no surprise that some lectins actually have beneficial activities under specific circumstances.

In fact, some lectins or lectin containing substances have been used in medicine (traditional and conventional) for a variety of purposes, primarily for their impact on the immune system. One of the largest uses of lectins by medical research is to convince certain immune cells to proliferate (a process called mitosis). Another common use of lectins is as a probe or tool to identify cancer cells. This is the area where the Helix pomatia snail overlaps the gray area between food and medicine. Coincidentally, snail has a historic reputation as an anti-cancer food.


Helix aspersa is known primarily for possessing a lectin (Helix Pomatia Agglutinin, or HPA) that has a variety of beneficial activities.

Larch Arabinogalactan.  Larch was added to this supplement as a way of modulating the microbiome to help make the immune system more robust. For example Larch has been shown to increase the production of short-chain fatty acids (SCFA’s), principally butyrate and propionate. These special fatty acids are critically important for the health of the colon. Larch has also been shown to modulation Natural Killer Cell and Macrophage activity via interferon gamma, tumor necrosis factor alpha, interleukin-1 beta (IL-1 beta) and IL-6. (5-9)

Helix aspersa
Larch arabinogalactan

TABLE 1: Key agents in Helix Plus.


Surface glycosylation (the expression of the glycoproteins--such as the ABO antigens, or blood group MN antigens), which in normal cells is very precisely controlled, is often defective in cancer cells. The result is the elaboration of tremendous amounts of incomplete or altered glycoproteins, many of which (including tumor markers like CA-125, CA15-3, CA 19-9, T, and Tn) have clinical and diagnostic relevance. The most readily recognized example of a surface glycosylation product is the ABO blood types. In a simple sense, ‘glycoprotein’ infers a molecule or chain made of an amino sugar and another carbohydrate sugar. Blood type antigens (A, B, O, or AB markers) are a real world example of a glycoprotein.

Nature employs these specialized glycoprotein chains to create structures that act as carriers of biological information. The few monosaccharides (or simple sugars like galactose, mannose, fucose, etc.) and amino sugars (like glucosamine, N-acetylgalactosamine) act almost like letters in an alphabet. Different combinations and lengths act to create a vocabulary of biological information. This biological information is then built onto the surface of your cell. In effect this creates our cell’s vocabulary and allows the cell to communicate and interact with their environment. Cell-to-cell adhesion is a critical role for surface glycoproteins.

On a healthy cell ABO antigens are clearly visible, but in diseased cells (like cancer cells), ABO antigens can often disappear or paradoxically be manufactured in enormous amounts. This results from the cancer cell being unable to completely assemble a normal, healthy glycoprotein on its surface.

In 1987 and 1991, Brooks and co-workers reported that it is possible to predict lymph node involvement in women with breast cancer by the detection of altered surface glycosylation. (1,2) Their 1991 study was performed on sections of 373 primary breast cancers, in a 24-year retrospective study. They found that the lectin, found in Helix aspsersa, is extremely specific for attaching to or identifying cells with these improperly assembled (compared with a healthy cell) glycoproteins.

It appears that as breast cells become malignant and more prone to metastasis, their surface glycosylation products alter in a predictable manner, resulting in elaboration of markers characterized by the presence of a terminal sugar which can make the cell appear very A-like and M-like to your immune system. (3) These changes result from the elaboration of a protein often referred to as ‘ligand-like complex’ or LLC. Manufacturing this protein may make it easier for the cancer cells to spread throughout the body because it acts like a ‘molecular passport’ allowing the cancer cell to more easily exit the lymph nodes. This can make the cell much more difficult for the immune system to recognize, especially for blood types A, AB and MM.

Let’s put this into a metaphorical picture to wrap up our discussion. Because cancer cells need to escape detection by your immune system in order to spread through your lymphatic system to distant parts of your body, anything that can be done to make cancer cells more visible to your immune system offers a potential advantage. In a sense, these altered glycosylation products on cancer cells may act very similar to a “cloaking device”, allowing the cancer cells to travel through the lymphatic system without detection by the immune system.

The lectin in Helix aspsersa, through its ability to recognize the altered glycosylation products on metastatic cells, appears to act in a similar way, turning off the cancer cells “cloaking device” and allowing it to be more visible to your immune system. As such, this food looks to be a good food to include in the diet, especially for A’s and AB’s.

Helix Plus is most often used in the management of malignant or neo-malignant states.


Typical dosage is 2 capsules twice daily, best taken away from meals.


This product was introduced by NAP in 1999 after first being specifically designed for use in The D’Adamo Clinic.


  1. Brooks SA. Lancet May 9, 1987: 1054-56
  2. Brooks SA and Leathem AJC. Lancet, 8759, 338 (1991): 71-74
  3. Springer G. J. Nat. Cancer Inst. 54,2 (1975):335-3
  4. Schumacher DU. et al. Eur. J. Surgical Oncology; 22(6) 1996:618-620
  5. Hauer J Anderer FA. Mechanism of stimulation of human natural killer cytotoxicity by arabinogalactan from Larix occidentalis. Cancer Immunol Immunother (1993) 36(4):237-44
  6. Vince AJ McNeil NI Wager JD Wrong OM. The effect of lactulose, pectin, arabinogalactan and cellulose on the production of organic acids and metabolism of ammonia by intestinal bacteria in a faecal incubation system. Br JNutr (1990 Jan) 63(1):17-26
  7. Englyst HN, Hay S, Macfarlane GT. Polysaccharide breakdown by mixed populations of human faecal bacteria. FEMS Microbiology Ecology (1987) 95: 163-71
  8. Salyers AA Arthur R Kuritza A. Digestion of larch arabinogalactan by a strain of human colonic. Bacteroides growing in continuous culture. J Agric Food Chem (1981 May-Jun) 29(3):475-80 (10)
  9. Svensson, S et al. Arabinogalactans, their preparation and compositions using same. European Patent Application Pub # 0138784 A2. European Patent Office. Filing Date: 8/20/84

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