Helicobacter pylori is a significant human pathogen known to colonise the human stomach. All cases of colonisation with H. pylori result in gastritis and H. pylori has been classified as a group 1 carcinogen by the WHO. Current treatment for H. pylori involves triple or quadruple antibiotic therapy, but antibiotic resistance is becoming increasingly prevalent. H. pylori has been found to interact with a group of carbohydrate histo-blood group antigens, known as the Lewis system antigens, via its adhesion proteins such as the blood group binding adhesin (BabA). Additionally, H. pylori has been found to express Lewis system antigens as a part of its lipopolysaccharide (LPS), which is thought to occur as a form of molecular mimicry. The structural diversity and variation of the H. pylori LPS presents a challenge in establishing an accurate structure-function relationship between the H. pylori LPS and an infected host. Further study into the expression and role of glycans in H. pylori infection and adhesion can shed new light on the molecular interactions of this bacterium and may lead to new drug and vaccination targets. This study has looked at profiling the glycan expression of H. pylori reference strains using monoclonal antibodies (mAbs) and lectins, identifying interaction between anti-Ley and anti-αGalactose mAbs and H. pylori strains SS1 and 26695. Both reference strains of H. pylori interacted with the mannose binding lectin Con A, and the N-acetylglucosamine and sialic acid binding lectin WGA. Additionally, the adhesive force of anti-Ley and WGA for intact H. pylori bacteria has been evaluated using atomic force microscopy (AFM). Both anti-Ley and WGA displayed adhesion with surface exposed glycans on the H. pylori curved rods, but flagella were not visible in the AFM scans. Further study will examine how carbohydrate binding proteins can affect the interaction between H. pylori reference strains and AGS cells in cell culture.