Reviews & Perspectives
Calculating Glycoprotein Similarities From Mass Spectrometric Data
In Brief To understand the roles of glycoproteins in biological processes, it is necessary to quantify the changes that occur to glycosylation at individual sites and to the whole molecule. That glycoprotein glycosylation is inherently heterogeneous means that the distribution of glycoforms at each glycosite must be quantified in order to inform calculation of molecular similarities. We review analytical and statistical methods for determining glycoprotein molecular similarities from glycoproteomics data.Why Glycosylation Matters in Building a Better Flu Vaccine
Immunodominant influenza A virus (IAV) antigens mutate rapidly, allowing the virus to escape host antibodies. The question remains how to design vaccines that recognize conserved but subdominant IAV antigens for broader immune protection. Glycosylation is a mechanism whereby IAV evades the innate and adaptive immune systems. However, its influence on immunodominance remains poorly understood. Although mass spectrometry methods for identifying glycopeptides are maturing, quantifying glycosylation variation among sets of IAV mutants remains a technical challenge.Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules
Extracellular networks of matrisome proteins and their binding partners give rise to dynamic cell and tissue-specific microenvironments. The extreme complexity of matrisome molecule glycosylation and other post-translational modifications belies the need for specialized omics methods. It is necessary to map the modifications of matrisome molecules in detail in order to understand their roles in normal and pathological physiology. We review proteomics, glycomics and glycoproteomics methods for matrisome molecules toward the goal of achieving detailed matrisome maps.
