Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310029, China.
Published: August 2005
AI Article Synopsis
Article Abstract
In this paper, recombinant human lactoferrin (rhLf) was expressed very well using Bombyx mori nuclear polyhedrosis baculovirus expression system. Infection of silkworm larvae with recombinant virus, vBm-hLf, the rhLf was efficiently secreted into larvae hemolymph and the concentration of product purified was about 65 microg/ml. The isolated rhLf molecular mass was approximately 78 kDa, lower than that of the human lactoferrin (hLf) standards, which may be due to incomplete glycosylation or protein degradation. Furthermore, the rhLf was characterized and its biological activities were evaluated by in vivo bioassay using dextran sodium sulfate (DSS)-induced colitis mouse model that mimics some characteristics of colitis disease in human. We conclude that silkworm expression system can be used successfully to express functional human lactoferrin.
Antimicrobial peptides (AMPs) are crucial constituents of inherent immunity and serve as vital components of human host defense, playing a pivotal role in combating invading microbial pathogens. Beyond their antimicrobial functions, AMPs also exhibit various other biological activities including apoptosis induction, wound healing promotion, and immune modulation. These peptides are found in various exposed tissues or surfaces throughout the body, such as eyes, skin, mouth, ears, respiratory tract, lungs, digestive, and urinary system.
Background: Subclinical mastitis is an asymptomatic inflammatory condition of the lactating mammary glands possibly associated with premature interruption of breastfeeding and poor weight gain in infants. However, data on human milk composition in mothers with subclinical mastitis are limited and inconsistent. Although human milk from donors with subclinical mastitis may be used after pasteurization if it meets the criteria, whether the composition is suitable for donor human milk remains unknown.
Background/objectives: Lactoferrin (Lf) is an iron-binding glycoprotein with multiple bioactivities, including promotion of cell proliferation and differentiation, immunomodulation, and antimicrobial activity. Lf, a basic glycoprotein, can bind to α-lactalbumin (α-Lac), an acidic whey protein. The current study aimed to evaluate whether Lf forms protein complexes with α-Lac and proteins/peptides from whey protein hydrolysate (WPH) and nonfat bovine milk powder (MP) and whether forming protein complexes influences resistance to gastrointestinal digestion and affects the bioactivities of Lf in human intestinal epithelial cells (HIECs and differentiated Caco-2 cells).
The immature gastrointestinal tract of preterm neonates leads to a delayed and distinctive establishment of the gut microbiome, making them susceptible to potentially pathogenic bacteria and increasing the risk of infections. Maternal milk, recognized as the optimal source of nutrition, plays a multifaceted role in modulating the gut microbiome of premature newborns. Human milk oligosaccharides, acting as prebiotics, provide essential nourishment for key bacteria such as Bifidobacterium, contributing to the proliferation of beneficial bacterial populations.
Avian pathogenic Escherichia coli (APEC) infections result in significant economic losses and reduced animal welfare. Historically, antibiotics and vaccinations currently control APEC infections in poultry, however, antibiotic-resistant strains and heterologous serotypes limit their effectiveness. Meanwhile, antibiotic-resistant strains can be transmitted to humans via contact with animals, food or their environment.
