The human immune system has the ability to distinguish between an extremely large number of pathogens. The human body has also developed a series of complex checkpoints and signals in order to distinguish between self and non-self antigens. Self-like microbes, those presenting human-like antigens on their surface, are in essence “hidden” from our natural immune response by utilizing a gap in our bodies innate immune system. The Stowell lab has previously shown that galectins (“Gals”), a β-galactoside sugar binding family of proteins found naturally in humans and other mammalian species, play a key role in the innate immune response to these self-like antigens 1. It has been demonstrated that both Gal-8 and Gal-4, each proteins consisting of 2 tandem homologous domains (figure1), are effective at targeting self-like antigens 2. Klebsiella pneumoniae (KP01) is a gram negative bacteria that alters its membrane lipopolysaccharides (LPS) to resemble that of mammalian cell membrane proteins such as blood group antigens 3. KP01’s LPS share terminal carbohydrates with that of blood group B antigens as they are presented on human cells (figure 2). This allows KP01 to take advantage of a hole in our innate immune system. Galectin proteins help fill this void and protect from infection. This study was conducted to determine if Gal-9 will cause killing of self-like microbes presenting blood group B antigens.

Investigating antimicrobial properties of the human galectin-9

253rd National Meeting (2017)

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