Antimicrobial effect of human milk on Bordetella pertussis

Redhead, Keith; Hill, Teresa

doi:10.1111/j.1574-6968.1990.tb13987.x

Cited by 7 publications

(6 citation statements)

References 22 publications

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“…Milk contains a wide array of antimicrobial sIgAs specific for bacterial, viral, and protozoal antigens (Redhead et al, 1990;Gillin et al, 1983), which reach mucosal surfaces of intestinal and respiratory tracts. Both mucosal and systemic immune response are barely developed in newborns, so mother's breast milk Abs ensure their protection against diseases for the first months of life (Newman, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the beginning of the lactation may be considered as an important period associated with the production of different Abzs. The mother's milk sIgA is active at the mucosal surfaces protecting the mucosa from the invasion of pathogenic microorganisms and limiting the access of environmental antigens (Redhead et al, 1990;Gillin et al, 1983). Therefore, Abzs could also contribute to the protective role of Abs through hydrolysis of different nucleic acids, polysaccharides (Nevinsky et al, 2002a(Nevinsky et al, ,b, 2003(Nevinsky et al, , 2005, and probably proteins.…”

Section: Introductionmentioning

confidence: 97%

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Casein-hydrolyzing activity of sIgA antibodies from human milk

2005

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During pregnancy and immediately after delivery (i.e. at the beginning of lactation), the female organism is frequently characterized by an immune status similar to that of patients with autoimmune diseases. In addition, lactation is associated with an appearance of catalytically active antibodies or abzymes (Abzs) with DNAse, RNase, ATPase, amylolitic, protein kinase and lipid kinase activities in breast milk. However, until now there were no examples of human milk Abzs with a proteolytic activity. We present the first evidence that electrophoretically and immunologically homogeneous human milk sIgAs possess a beta-casein-hydrolyzing activity different from known proteases. Abzs specifically hydrolyze both human and bovine beta-caseins but not many other proteins tested. Using different methods including in situ analysis of proteolytic activity in a gel after SDS-PAGE it was shown that the observed proteolytic activity is an intrinsic property of human milk polyclonal sIgAs. Specific inhibitors of acidic and thiol proteases demonstrated a weak effect on proteolytic activity of Abzs, while a specific inhibitor of serine proteases (AEBSF) significantly inhibited the proteolytic activity of the abzymes. The K(M) value for human casein as a substrate was estimated (7.3 microM). Our findings suggest that the immune system of clinically healthy mothers can generate IgAs with a beta-casein-specific serine protease-like activity.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

Casein-hydrolyzing activity of sIgA antibodies from human milk

2005

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“…At levels between 10 and 200 mg per litre of medium, lysozyme was effective against bacteria involved in food-borne disease and food spoilage (Hughey and Johnson, 1987). Additionally, it has been shown that human milk is more effective at stopping the growth of Bacillus pertussis than is bovine milk (Redhead et al, 1990). At 100 mg per litre of milk, lysozyme was effective at inhibiting the growth of nonacid-forming bacteria (Panfil-Kuncewicz and Kisza, 1976).…”

Section: Introductionmentioning

confidence: 97%

Expression of human lysozyme mRNA in the mammary gland of transgenic mice

Maga

Anderson

Huang

et al. 1994

Transgenic Research

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Owing to its inherent antimicrobial effect and positive charge, the expression of human lysozyme in bovine milk could be beneficial by altering the overall microbial level and the functional and physical properties of the milk. We have used transgenic mice as model systems to evaluate the expression of human lysozyme containing fusion gene constructs in the mammary gland. Expression of human lysozyme was targeted to the mammary gland by using the 5' promoter elements of either the bovine beta (line B mice) or alpha s1 (line H mice) casein genes coupled to the cDNA for human lysozyme. Expression of human lysozyme mRNA was not found in mammary tissue from any of line B mice. Tissues were analysed from six lines of H mice and two, H6 and H5, were found to express human lysozyme mRNA in the mammary gland at 42% and 116%, respectively, of the levels of the endogenous mouse whey acidic protein gene. At peak lactation, female mice homozygous for the H5 and H6 transgene have approximately twice the amount of mRNA encoding human lysozyme as hemizygous animals. Expression levels of human lysozyme mRNA in the mammary gland at time points representing late pregnancy, early, peak and late lactation corresponded to the profile of casein gene expression. Human lysozyme mRNA expression was not observed in transgenic males, virgin females or in the kidney, liver, spleen or brain of lactating females. A very low level of expression of human lysozyme mRNA was observed in the salivary gland of line H5.

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“…Human milk provides the breast‐fed child not just with nutrients, but with a mucosal immune system. Milk contains a wide array of molecules with antimicrobial activity: antibodies to bacterial, viral and protozoal antigens (Gillin et al ., 1983; Hanson et al ., 1985; Redhead et al ., 1990; Ogra and Rassin, 1995); bactericidal molecules such as lysozyme and lactoferrin (Reiter, 1984; Lönnerdal, 1985); fatty acids that lyse bacteria and viral particles (Kabara et al ., 1972; Sarkar et al ., 1973; Kabara, 1980); and glycoconjugates that inhibit bacterial adherence to epithelial cells (Andersson et al ., 1983; Svanborg et al ., 1991; Kunz and Rudloff, 1993; Newburg, 1999). These components reach mucosal surfaces in the respiratory and gastrointestinal tracts of the breast‐fed child and are thought to interfere with various steps in disease pathogenesis at these sites (Ofek et al ., 1977; Andersson et al ., 1986; Kunz and Rudloff, 1993).…”

Section: Introductionmentioning

confidence: 99%

A folding variant of α‐lactalbumin with bactericidal activity against Streptococcus pneumoniae

Håkansson

Svensson

Mossberg

et al. 2000

Molecular Microbiology

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SummaryThis study describes an a-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was puri®ed from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was retained on the ion-exchange matrix and eluted only with high salt. The eluted fraction showed N-terminal and mass spectrometric identity with human milk a-lactalbumin, but native alactalbumin had no bactericidal effect. Spectroscopic analysis demonstrated that the active form of the molecule was in a different folding state, with secondary structure identical to a-lactalbumin from human milk whey, but¯uctuating tertiary structure. Native a-lactalbumin could be converted to the active bactericidal form by ion-exchange chromatography in the presence of a cofactor from human milk casein, characterized as a C18:1 fatty acid. Analysis of the antibacterial spectrum showed selectivity for streptococci; Gram-negative and other Gram-positive bacteria were resistant. The folding variant of a-lactalbumin is a new example of naturally occurring molecules with antimicrobial activity.

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Antimicrobial effect of human milk on Bordetella pertussis

Cited by 7 publications

References 22 publications

Casein-hydrolyzing activity of sIgA antibodies from human milk

Casein-hydrolyzing activity of sIgA antibodies from human milk

Expression of human lysozyme mRNA in the mammary gland of transgenic mice

A folding variant of α‐lactalbumin with bactericidal activity against Streptococcus pneumoniae

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