Candida glabrata (CG) is an opportunistic fungal pathogen that initiates infection by binding to host cells via specific lectin-like adhesins proteins. We have previously shown the importance of lectin-oligosaccharide binding in cardiac responses to flow and agonists. Due to the lectinic-oligosaccharide nature of CG binding, we tested the ability of CG to alter the agonist- and flow-induced changes in cardiac function in isolated perfused guinea pig hearts. Both transmission and scanning electron microscopy showed strong attachment of CG to the coronary endothelium, even after extensive washing. CG shifted the coronary flow versus AV-delay relationship upward, indicating that greater flow was required to achieve the same AV delay. This effect was completely reversed with mannose, partially reversed with galactose and N- acetylgalactosamine, but hyaluronan had no effect. Western blot was used to determine binding of CG to isolated coronary endothelial luminal membrane (CELM) receptors and the results indicate that flow sensitive CELM receptors, Angiotensin II type I, α- adrenergic 1A, endothelin-2 and VCAM-1 bind to CG. In addition, CG inhibited agonist-induced effects of bradykinin, angiotensin and phenylephrine on AV delay, coronary perfusion pressure and left ventricular pressure. Mannose reversed the inhibitory effects of CG on the agonist responses. These results suggest that CG directly binds to flow sensitive CELM receptors via lectinic-oligosaccharide interactions with mannose and disrupts the lectin-oligosaccharide binding necessary for flow-induced cardiac responses.