The occurrence and production of avidin: a new conception of the high-affinity biotin-binding protein

Elo, Heikki A.; Korpela, Jukka

doi:10.1016/0305-0491(84)90137-8

Cited by 26 publications

(18 citation statements)

References 55 publications

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“…Similarly, the host innate immune system has been shown to target biotin. Chicken embryo fibroblasts and yolk-sac macrophages induce the production of avidin, which binds and sequesters biotin in response to Escherichia coli infection, treatment with lipopolysaccharide (LPS), or interleukin-6 (32,33). These data suggest that sequestration of biotin may be a form of nutritional immunity by the host innate immune system and support the idea that biotin might be a critical and limited commodity during infection.…”

Section: Discussionmentioning

confidence: 99%

Link between intraphagosomal biotin and rapid phagosomal escape in Francisella

Napier

Meyer

Bina

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Cytosolic bacterial pathogens require extensive metabolic adaptations within the host to replicate intracellularly and cause disease. In phagocytic cells such as macrophages, these pathogens must respond rapidly to nutrient limitation within the harsh environment of the phagosome. Many cytosolic pathogens escape the phagosome quickly (15-60 min) and thereby subvert this host defense, reaching the cytosol where they can replicate. Although a great deal of research has focused on strategies used by bacteria to resist antimicrobial phagosomal defenses and transiently pass through this compartment, the metabolic requirements of bacteria in the phagosome are largely uncharacterized. We previously identified a Francisella protein, FTN_0818, as being essential for intracellular replication and involved in virulence in vivo. We now show that FTN_0818 is involved in biotin biosynthesis and required for rapid escape from the Francisella-containing phagosome (FCP). Addition of biotin complemented the phagosomal escape defect of the FTN_0818 mutant, demonstrating that biotin is critical for promoting rapid escape during the short time that the bacteria are in the phagosome. Biotin also rescued the attenuation of the FTN_0818 mutant during infection in vitro and in vivo, highlighting the importance of this process. The key role of biotin in phagosomal escape implies biotin may be a limiting factor during infection. We demonstrate that a bacterial metabolite is required for phagosomal escape of an intracellular pathogen, providing insight into the link between bacterial metabolism and virulence, likely serving as a paradigm for other cytosolic pathogens. S ubversion of the hostile phagosomal environment is required for the survival of intracellular bacteria. Although bacterial strategies to resist antimicrobial phagosomal defenses have been studied in great detail (1, 2), the ways in which bacteria counter phagosomal nutrient limitation are largely unknown. This is especially true for cytosolic pathogens that are often in the phagosome for a very limited time (15-60 min), before escaping this compartment to reach their replicative niche in the cytoplasm. During this brief and dynamic time, it is unclear if cytosolic pathogens require sequestration of nutrients or synthesis of de novo metabolites to promote their virulence strategies and escape the toxic phagosome.Francisella tularensis is a cytosolic intracellular Gram-negative bacterial pathogen that uses a multitude of mechanisms to evade phagosomal host defenses (3). This pathogen is highly virulent and causes the potentially fatal disease tularemia. Francisella novicida U112 and Francisella holarctica LVS (live vaccine strain) are less virulent yet highly related strains that are often used as models to study F. tularensis. Like other cytosolic bacterial pathogens, after initial contact with the host macrophage, Francisella spp. are taken up into a phagosome and rapidly escape (30-60 min) this compartment to reach and replicate within the cytosol (3-5). The mechanism by w...

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Section: Discussionmentioning

confidence: 99%

Link between intraphagosomal biotin and rapid phagosomal escape in Francisella

Napier

Meyer

Bina

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…This characteristic property of avidin is widely used in chemical and immunological assays and diagnosis. The high binding activity of avidin to biotin explains the efficacy to inhibit bacterial growth [24]. The strong binding of avidin and biotin can be used for one-step separation of avidin from egg white using biocytin-conjugated affinity chromatography [25].…”

Section: B) Eggmentioning

confidence: 99%

Bioactive Proteins and Peptides from Food Sources. Applications of Bioprocesses used in Isolation and Recovery

Kitts

Weiler²

2003

CPD

774

411

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There are many examples of biologically active food proteins, with physiological significance beyond the pure nutritional requirements that concern available nitrogen for normal growth and maintenance. Moreover, there are many physiologically active peptides, derived by protease activity from various food protein sources; however, relationships between structural properties and functional activities have not been completely elucidated. Many bioactive peptides have in common structural properties that include a relatively short peptide residue length (e.g. 2-9 amino acids), possessing hydrophobic amino acid residues in addition to proline, lysine or arginine groups. Bioactive peptides are also resistant to the action of digestion peptidases. Antihypertensive peptides, known as Angiotensin I converting enzyme (ACE) inhibitors have been derived from milk, corn and fish protein sources. Peptides with opioid activities are derived from wheat gluten or casein, following digestion with pepsin. Exorphins, or opioid peptides derived from food proteins such as wheat and milk (e.g. exogenous sources) have similar structure to endogenous opioid peptides, with a tyrosine residue located at the amino terminal or bioactive site. Immunomodulatory peptides derived from tryptic hydrolysates of rice and soybean proteins act to stimulate superoxide anions (reactive oxygen species-ROS), which triggers non-specific immune defense systems. Antioxidant properties that prevent peroxidation of essential fatty acids have also been shown for peptides derived from milk proteins. The addition of a Leu or Pro residue to the N-terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants (e.g. BHT). We also show herein, that the tryptic digests of casein yielding caseinophosphopeptides exhibits both hydrophilic and lipophilic antioxidant activity due to both metal ion sequestering and quenching of ROS. The separation and purification of bioactive peptides which will involve development of automated and continuous systems is an important field for Food chemists. Much effort has been given to develop selective column chromatography methods that can replace batch methods of salting out, or using solvent extraction to isolate and purify bioactive peptides. Advances here will enable recovery of bioactive peptides with minimal destruction thus enabling utilization by returning these active peptides to functional food or specific nutraceutical applications.

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“…This is not surprising, since BEs are generally intracellular molecules (Duhamel and Whitehead 1990) that do not come into contact with the host immune system while the cell membrane is intact [though some bacteria, including Escherichia coli, express biotin-containing components at their surface (Elo and Korpela 1984)]. In immunization the antibody response to BE was Fig.…”

Section: Discussionmentioning

confidence: 98%

Analysis of the antigenicity in mice of biotinyl enzymes from Anisakis simplex and other nematodes

Lorenzo

Iglesias

Paniagua

et al. 1999

Parasitology Research

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We analyzed the antigenicity of biotinyl enzymes contained in somatic extracts from Anisakis simplex and other parasite nematodes and show in this report that these molecules are an important source of cross-reactivity problems among these nematodes. Cross-reactivity was most pronounced among members of the superfamily Ascaridoidea. These results suggest that the presence of biotinyl enzymes in whole somatic extracts of A. simplex and other parasites may make serodiagnostic assays based on this kind of antigenic preparation unreliable.

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The occurrence and production of avidin: a new conception of the high-affinity biotin-binding protein

Cited by 26 publications

References 55 publications

Link between intraphagosomal biotin and rapid phagosomal escape in Francisella

Link between intraphagosomal biotin and rapid phagosomal escape in Francisella

Bioactive Proteins and Peptides from Food Sources. Applications of Bioprocesses used in Isolation and Recovery

Analysis of the antigenicity in mice of biotinyl enzymes from Anisakis simplex and other nematodes

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