Streptococcus pyogenes (group A streptococcus; GAS) is responsible for approximately 700 million cases of localised infection and 600,000 cases of invasive infection globally each year. Over the past three decades there has been a resurgence in GAS invasive disease in Western countries, which has been paralleled by the emergence of the highly virulent M1T1 GAS clone. Serotype M1 GAS is among the most frequently isolated serotypes from streptococcal pharyngitis and necrotizing fasciitis worldwide. Intensive research has focused on the mechanisms that underlie the enhanced invasive propensity of this serotype, whilst fewer studies have focused on the mechanisms that underpin the initial interaction of M1 GAS with the host. The first stage of bacterial infection is initiated by the specific recognition of host epithelial surfaces. Many pathogenic and commensal microbes exploit cell surface glycans as ligands for cell attachment, colonisation and invasion. GAS typically colonises epithelial cells of the skin and mucosal surfaces, where they it is likely to encounter a diverse array of glycosylated structures. Despite this, interactions between GAS and host glycans remain poorly characterised. Using a high throughput approach, we have determined that the GAS cell surface M1 protein displays novel lectin characteristics, with a high affinity for glycans containing a Galβ1-3GlcNAcβ1-3Gal core. Furthermore, we have shown that the globally disseminated M1T1 GAS strain 5448 interacts with specific host glycans in an M protein dependant manner. Glycan binding by GAS was found to enhance bacterial attachment to human pharyngeal cells. We hypothesise that the globally disseminated M1T1 GAS has evolved unique, M protein dependant mechanisms for interacting with specific host glycan structures, and that these interactions contribute to colonisation and persistence in the throat.