Human Milk Secretory Antibodies against Attaching and Effacing<i>Escherichia coli</i>Antigens

Noguera-Obenza, Marita; Ochoa, Theresa J.; Gomez, Henry F.; Guerrero, M. Lourdes; Herrera-Insua, Irene; Morrow, Ardythe L.; Ruíz-Palacios, Guillermo M.; Pickering, Larry K.; Guzmán, Carlos A.; Cleary, Thomas G.

doi:10.3201/eid0905.020441

Cited by 40 publications

(23 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The recognition of the 94 kDa band of STEC O157 was weaker than that of STEC O111, probably due to the lower incidence of this serotype in Brazil. The presence of anti-intimin IgA antibodies was detected in milk samples of women from Mexico and United States, even in regions with low frequency of bacterial diarrhoea [23].…”

Section: Discussionmentioning

confidence: 99%

Colostrum from healthy Brazilian women inhibits adhesion and contains IgA antibodies reactive with Shiga toxin-producing Escherichia coli

et al. 2005

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Colostrum from healthy Brazilian women inhibits adhesion and contains IgA antibodies reactive with Shiga toxin-producing Escherichia coli

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Children infected with EPEC have serum immunoglobulin G (IgG) against intimin, EspA, and EspB (38). Moreover, human milk contains antibodies to intimin, EspA, EspB, and Tir (36,37,41,42,45). Breastfeeding protects infants from respiratory and intestinal infections (25,26,54), including EPEC (4).…”

mentioning

confidence: 99%

Lactoferrin Impairs Type III Secretory System Function in EnteropathogenicEscherichia coli

Ochoa

Noguera-Obenza

Ebel³

et al. 2003

Infect Immun

Self Cite

View full text Add to dashboard Cite

Enteropathogenic Escherichia coli (EPEC) is an important cause of infant diarrhea in developing countries. EPEC uses a type III secretory system to deliver effector proteins into the host cell. These proteins cause the characteristic attaching and effacing lesion on enterocytes. Lactoferrin, a glycoprotein present in human milk, inhibits EPEC adherence to mammalian cells. To determine the effect of lactoferrin on the initial host cell attachment step that is mediated by the type III secretory system, we focused on EPEC-induced actin polymerization in HEp2 cells, on the hemolytic activity, and on measurement of E. coli secreted proteins A, B, and D (EspABD). Lactoferrin blocked EPEC-mediated actin polymerization in HEp2 cells and blocked EPEC-induced hemolysis. The mechanism of this inhibition was lactoferrin-mediated degradation of secreted proteins necessary for bacterial contact and pore formation, particularly EspB. The proteolytic effect of lactoferrin was prevented by serine protease inhibitors. This disruption of the type III secretory system implies that lactoferrin could provide broad cross protection against the enteropathogens that share this mechanism.Enteropathogenic Escherichia coli (EPEC) is one of the major causes of infant diarrhea in developing countries. EPEC usually produces an acute watery diarrhea, but it can produce chronic diarrhea and lead to malnutrition (39).EPEC induces a distinctive histopathology known as the attaching and effacing lesion, which is characterized by the intimate attachment of bacteria to the epithelial surface and the effacement of host cell microvilli. There are three stages in EPEC pathogenesis: (i) initial adherence to the host cell through the bundle-forming pilus, (ii) production and translocation of bacterial proteins through a needle complex via a type III secretory system, and (iii) actin polymerization-associated intimate attachment and pedestal formation (20,39,53).The type III secretory system is present in many pathogenic gram-negative bacteria (Salmonella, Shigella, and Yersinia spp., Shiga toxin-producing E. coli, and Pseudomonas spp.). Its function is to transport virulence proteins from the bacterial cytoplasm into the host cell plasma membrane and cytoplasm upon contact with target cells (14,20,24). In EPEC, the type III secretory system forms a needle complex made of E. coli secretion component F (EscF), which is anchored to the inner and outer membranes of the bacteria through an inner and outer ring. Multimers of E. coli secreted protein A (EspA) attach to the tip of the needle, forming a tube-like structure between the bacterium and the host cell. Bacterial proteins (EspB, EspD, translocated intimin receptor [Tir], and others) are introduced into the mammalian cell via this tube. EspB and EspD create pores in the eukaryotic cell membrane. Intimin, an outer membrane bacterial protein binds to its receptor Tir, following the translocation and surface expression of Tir on the host cell. Intimin-Tir binding triggers polymerization of actin and other c...

show abstract

“…The immunogenicity of the LEE-encoded proteins studied here was also observed in patients infected with E. coli O157:H7 or other EHEC serotypes, as well as in their household contacts (13,18) or children with EPEC-associated diarrhea (23). Furthermore, several studies have shown that colostrum and milk from healthy women from both industrialized and developing countries contain IgA antibodies reactive to the LEE-encoded proteins (20,22,30,33).…”

Section: Discussionmentioning

confidence: 79%

“…Antibodies against these proteins have also been detected in colostrum and milk from healthy women (20,22,30,33).…”

mentioning

confidence: 99%

Bovine Colostrum Contains Immunoglobulin G Antibodies against Intimin, EspA, and EspB and Inhibits Hemolytic Activity Mediated by the Type Three Secretion System of Attaching and Effacing Escherichia coli

Vilte

Larzábal

Cataldi

et al. 2008

Clin Vaccine Immunol

View full text Add to dashboard Cite

Enterohemorrhagic Escherichia coli (EHEC) is the main cause of hemolytic-uremic syndrome, an endemic disease in Argentina which had an incidence in 2005 of 13.9 cases per 100,000 children younger than 5 years old. Cattle appear to be a major reservoir of EHEC, and a serological response to EHEC antigens has been demonstrated in natural and experimental infections. In the current study, antibodies against proteins implicated in EHEC's ability to form attaching and effacing lesions, some of which are exported to the host cell via a type three secretion system (TTSS), were identified in bovine colostrum by Western blot analysis. Twenty-seven (77.0%) of the 35 samples examined contained immunoglobulin G (IgG) antibodies against the three proteins assayed in this study: EspA, EspB, and the carboxy-terminal 280 amino acids of ␥-intimin, an intimin subtype associated mainly with O157:H7 and O145:H-serotypes. Every colostrum sample was able to inhibit, in a range between 45.9 and 96.7%, the TTSS-mediated hemolytic activity of attaching and effacing E. coli. The inhibitory effect was partially mediated by IgG and lactoferrin. In conclusion, we found that early colostrum from cows contains antibodies, lactoferrin, and other unidentified substances that impair TTSS function in attaching and effacing E. coli strains. Bovine colostrum might act by reducing EHEC colonization in newborn calves and could be used as a prophylactic measure to protect non-breast-fed children against EHEC infection in an area of endemicity.

show abstract

Human Milk Secretory Antibodies against Attaching and EffacingEscherichia coliAntigens

Cited by 40 publications

References 40 publications

Colostrum from healthy Brazilian women inhibits adhesion and contains IgA antibodies reactive with Shiga toxin-producing Escherichia coli

Colostrum from healthy Brazilian women inhibits adhesion and contains IgA antibodies reactive with Shiga toxin-producing Escherichia coli

Lactoferrin Impairs Type III Secretory System Function in EnteropathogenicEscherichia coli

Bovine Colostrum Contains Immunoglobulin G Antibodies against Intimin, EspA, and EspB and Inhibits Hemolytic Activity Mediated by the Type Three Secretion System of Attaching and Effacing Escherichia coli

Contact Info

Product

Resources

About