Abstract
Human lysozyme is a natural non-specific immune factor in human milk that plays an important role in the defense of breastfed infants against pathogen infection. Although lysozyme is abundant in human milk, there is only trace quantities in pig milk. Here, we successfully generated transgenic cloned pigs with the expression vector pBAC-hLF-hLZ-Neo and their first generation hybrids (F1). The highest concentration of recombinant human lysozyme (rhLZ) with in vitro bioactivity was 2759.6 ± 265.0 mg/L in the milk of F0 sows. Compared with wild-type milk, rhLZ milk inhibited growth of Escherichia coli K88 during the exponential growth phase. Moreover, rhLZ in milk from transgenic sows was directly absorbed by the intestine of piglets with no observable anaphylactic reaction. Our strategy may provide a powerful tool for large-scale production of this important human protein in pigs to improve resistance to pathogen infection.
Highlights
Lysozyme is a natural, non-specific, immune factor, which widely exists in animals, plants, and microorganisms
Discussion human lysozyme (hLZ) is a major component in human milk and plays an important role in the innate immune response of breastfed infants against infection of pathogenic bacteria and viruses
We produced a herd of recombinant human lysozyme (rhLZ) transgenic cloned pigs with high rhLZ expression levels in milk
Summary
Non-specific, immune factor, which widely exists in animals, plants, and microorganisms. Lysozyme directly kills bacteria (especially Gram-positive species) through hydrolysis of tetrasaccharide β-(1!4)-glycosidic linkages in the cell wall [5]. Previous studies have indicated that lysozyme may possess a muramidase-independent mechanism to kill bacteria [1,6,7]. Since it received a status of “generally recognized as safe” by the World Health Organization and US Food and Drug Administration, lysozyme is used widely as a food preservative [8]. Previous experimental and clinical studies demonstrated that lysozyme can enhance the function and proliferation of polymorphonuclear neutrophils and PLOS ONE | DOI:10.1371/journal.pone.0123551 May 8, 2015
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