Can Mannose-Binding Lectin Activation Help in Fighting Bacterial Pathogen in Poultry Production Systems?—A Review

Abstract

Bacterial pathogens have been attributed to poultry housing structure, financial strength, and incessant use of antibiotics, variable seasons and management systems practiced. Variant forms of bacterial pathogens can be detected by recognizing the molecular pattern of the pathogens through an innate immune mechanism such as mannose-binding lectin. Mannose-binding lectin (MBL) possesses an innate pattern recognition molecule that easily sequestered to region of infections and inflammations. This works by attaching itself to antigen surface thus hinders proliferation and disease activity in the host organism. Baker’s method, nephelometric assays technique, Enzyme-Linked Immunosurbent Assay technique, Polymerase Chain Reaction, Deoxyribonucleic Acid typing and other biotechnology related methods are techniques used in detecting and quantifying MBL. Mannose-binding lectin levels in serum can be influenced by age, management systems, feed formulation strategies and seasons. Therefore, knowledge of MBL should be encouraged in all aspect of poultry production, in order to discourage incessant use of drugs at a slight exposure to prevailing bacterial which can help in maximizing cost.

Activity of Mannose-Binding Lectin on Bacterial-Infected Chickens—A Review

“…The neck domain initiates trimerization of the monomers which is stabilized by the intertwined collagen of MBL [ 9 , 20 ]. The trimer is considered the smallest active form of MBL (structurally, the smallest form of MBL) [ 20 ]. The N-terminal domains can covalently crosslink the MBL trimers via the cysteine residues, to higher oligomeric structures ( Figure 2 ).…”

“…The N-terminal domains can covalently crosslink the MBL trimers via the cysteine residues, to higher oligomeric structures ( Figure 2 ). The International Union of Immunological Societies (IUIS) had not defined a specific oligomeric structure for MBL, and, in nature, several forms of MBL are present across animal species [ 9 , 19 , 20 , 21 ]. Laursen et al [ 22 ] observed that purified chicken MBL has a similar structure as mammalian MBL [ 9 , 19 , 20 , 21 ].…”

“…MBL is a significant member of the PRR family with ability to recognize PAMPs ranging from microbial DNA/RNA to protein and membrane components of microbes [ 19 , 20 ]. This binding requires a calcium ion (characteristic for C-type lectins) which links the hydroxyl side chains of the sugar residue to specific amino acids in the binding pocket of the lectin domain [ 26 , 27 ].…”