(N)-linked protein glycosylation is a ubiquitous co- and post-translational modification which can alter the biological function of proteins and consequently affects the development, growth, and physiology of organisms. Despite an increasing knowledge of N-glycan biosynthesis and processing, very little is known about the biological function of individual N-glycan structures in plants. In particular, the N-glycan-processing steps mediated by Golgi-resident enzymes create a structurally diverse set of protein-linked carbohydrate structures. Some of these complex N-glycan modifications like the presence of β1, 2-xylose, core α1, 3-fucose or the Lewis a-epitope are characteristic for plants and are evolutionary highly conserved. In mammals, complex N-glycans are involved in different cellular processes including molecular recognition and signaling events. In contrast, the complex N-glycan function is still largely unknown in plants. Simple and complex carbohydrates (glycans) have long been known to play major metabolic, structural roles in biological systems. Targated microbial binding to host glycans has also been studied for decades. But such biological roles can only explain some of the remarkable complexity and organismal diversity of glycans in nature. It plays a critical role in host-pathogens interactions, antigenicity, and virulence determination and are therefore, considered as potential drug targets. The cell wall of Mycobacterium tuberculosis (Mtb) the causative agent of tuberculosis (TB), dominantly contains sugar and lipids. Despite the effort taken by the World Health Organization to reduce the incident rate, the prevalence of TB is increasing in certain regions. This short focuses on important recent developments and discuss their implications for future research in plant glycobiology and plant biotechnology.