Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria.
Interfacultary Institute of Biochemistry, University of Tuebingen, 72074 Tuebingen, Germany.
Biomolecules. 2020 Oct 22;10(11):1470. doi: 10.3390/biom10111470.
A number of studies have shown that glycosylation of proteins plays diverse functions in the lives of organisms, has crucial biological and physiological roles in pathogen-host interactions, and is involved in a large number of biological events in the immune system, and in virus and bacteria recognition. The large amount of scientific interest in glycoproteins of molluscan hemocyanins is due not only to their complex quaternary structures, but also to the great diversity of their oligosaccharide structures with a high carbohydrate content (2-9%). This great variety is due to their specific monosaccharide composition and different side chain composition. The determination of glycans and glycopeptides was performed with the most commonly used methods for the analysis of biomolecules, including peptides and proteins, including Matrix Assisted Laser Desorption/Ionisation-Time of Flight (MALDI-TOF-TOF), Liquid Chromatography - Electrospray Ionization-Mass Spectrometry (LC/ESI-MS), Liquid Chromatography (LC-Q-trap-MS/MS) or Nano- Electrospray Ionization-Mass Spectrometry (nano-ESI-MS) and others. The molluscan hemocyanins have complex carbohydrate structures with predominant -linked glycans. Of interest are identified structures with methylated hexoses and xyloses arranged at different positions in the carbohydrate moieties of molluscan hemocyanins. Novel acidic glycan structures with specific glycosylation positions, e.g., hemocyanins that enable a deeper insight into the glycosylation process, were observed in , , and . Recent studies demonstrate that glycosylation plays a crucial physiological role in the immunostimulatory and therapeutic effect of glycoproteins. The remarkable diversity of hemocyanin glycan content is an important feature of their immune function and provides a new concept in the antibody-antigen interaction through clustered carbohydrate epitopes.
许多研究表明，蛋白质的糖基化在生物体的生命中发挥着多样化的功能，在病原体-宿主相互作用中具有关键的生物学和生理学作用，并参与免疫系统中的大量生物事件，以及病毒和细菌的识别。科学界对软体动物血蓝蛋白糖蛋白的大量兴趣不仅源于其复杂的四级结构，还源于其具有高糖含量（2-9%）的寡糖结构的巨大多样性。这种多样性源于其特定的单糖组成和不同的侧链组成。糖链和糖肽的测定采用了最常用于分析生物分子的方法，包括肽和蛋白质，包括基质辅助激光解吸/电离-飞行时间（MALDI-TOF-TOF）、液相色谱-电喷雾电离-质谱（LC/ESI-MS）、液相色谱（LC-Q-trap-MS/MS）或纳升电喷雾电离-质谱（nano-ESI-MS）等。软体动物血蓝蛋白具有复杂的碳水化合物结构，主要为β-连接的聚糖。有趣的是，在软体动物血蓝蛋白碳水化合物部分的不同位置排列有甲基化的己糖和木糖的鉴定结构。在、和中观察到具有特定糖基化位置的新型酸性糖链结构，例如使人们能够更深入地了解糖基化过程的血蓝蛋白。最近的研究表明，糖基化在糖蛋白的免疫刺激和治疗作用中起着至关重要的生理作用。血蓝蛋白糖含量的显著多样性是其免疫功能的一个重要特征，并通过糖簇表位提供了抗体-抗原相互作用的新概念。
