Pathogen-Induced Glycosylation Alterations: Untangling the Host Cell’s Sweet Response

This chapter explores the intricate relationship between pathogens and host cell glycosylation alterations. Glycosylation, a crucial post-translational modification, plays a significant role in various cellular processes, including cell signaling, immune response, and pathogen recognition. Pathogens such as viruses, bacteria, and parasites have evolved diverse strategies to exploit and manipulate host cell glycosylation machinery, leading to changes in the glycomic profile. This chapter focuses on the glycosylation alterations induced by Helicobacter pylori, human papillomavirus, hepatitis B and C viruses, and human T-cell leukemia virus type 1, associated with cancer, SARS-CoV-2, and H1N1, implicated in lower respiratory infection, and Salmonella enterica and Escherichia coli, which cause diarrheal diseases. The review examines the impact of pathogen infection on host glycosylation by affecting the expression of glycogenes. In addition, pathogens may secrete glycosyltransferases or glycosidases that can directly modify host glycans, further contributing to glycomic changes. Besides, pathogens can modify the serum glycome associated with a specific pathogen infection or patient outcomes. This review provides valuable insights into the complex interactions between pathogens and host cell glycans, shedding light on the potential implications for disease progression and the development of targeted interventions.