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      Recent advances in the concept of paraprobiotics: Nutraceutical/functional properties for promoting children health

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          Maternal and child undernutrition: global and regional exposures and health consequences.

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            Host interactions of probiotic bacterial surface molecules: comparison with commensals and pathogens.

            How can probiotic bacteria transduce their health benefits to the host? Bacterial cell surface macromolecules are key factors in this beneficial microorganism-host crosstalk, as they can interact with host pattern recognition receptors (PRRs) of the gastrointestinal mucosa. In this Review, we highlight the documented signalling interactions of the surface molecules of probiotic bacteria (such as long surface appendages, polysaccharides and lipoteichoic acids) with PRRs. Research on host-probiotic interactions can benefit from well-documented host-microorganism studies that span the spectrum from pathogenicity to mutualism. Distinctions and parallels are therefore drawn with the interactions of similar molecules that are presented by gastrointestinal commensals and pathogens.
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              Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human- mucus binding protein.

              To unravel the biological function of the widely used probiotic bacterium Lactobacillus rhamnosus GG, we compared its 3.0-Mbp genome sequence with the similarly sized genome of L. rhamnosus LC705, an adjunct starter culture exhibiting reduced binding to mucus. Both genomes demonstrated high sequence identity and synteny. However, for both strains, genomic islands, 5 in GG and 4 in LC705, punctuated the colinearity. A significant number of strain-specific genes were predicted in these islands (80 in GG and 72 in LC705). The GG-specific islands included genes coding for bacteriophage components, sugar metabolism and transport, and exopolysaccharide biosynthesis. One island only found in L. rhamnosus GG contained genes for 3 secreted LPXTG-like pilins (spaCBA) and a pilin-dedicated sortase. Using anti-SpaC antibodies, the physical presence of cell wall-bound pili was confirmed by immunoblotting. Immunogold electron microscopy showed that the SpaC pilin is located at the pilus tip but also sporadically throughout the structure. Moreover, the adherence of strain GG to human intestinal mucus was blocked by SpaC antiserum and abolished in a mutant carrying an inactivated spaC gene. Similarly, binding to mucus was demonstrated for the purified SpaC protein. We conclude that the presence of SpaC is essential for the mucus interaction of L. rhamnosus GG and likely explains its ability to persist in the human intestinal tract longer than LC705 during an intervention trial. The presence of mucus-binding pili on the surface of a nonpathogenic Gram-positive bacterial strain reveals a previously undescribed mechanism for the interaction of selected probiotic lactobacilli with host tissues.
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                Author and article information

                Contributors
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                Journal
                Critical Reviews in Food Science and Nutrition
                Critical Reviews in Food Science and Nutrition
                Informa UK Limited
                1040-8398
                1549-7852
                November 08 2021
                : 1-16
                Affiliations
                [1 ]School of Bioengineering & Food Technology, Shoolini University of Biotechnology and Management Sciences, Solan, India
                [2 ]Department of Medicine/Biomedicine, Faculty of Medicine, University of Porto, Porto, Portugal
                [3 ]School of Biological and Environmental Sciences, Shoolini University of Biotechnology and Management Sciences, Solan, India
                [4 ]Department of Chemistry, Faculty of Science, University of Hradec Kralove, Hradec Kralove, Czech Republic
                [5 ]School of Bioengineering and Biosciences, Lovely Professional University, Phagwara, Punjab, India
                [6 ]Institute for Research and Innovation in Health (i3S), University of Porto, Porto, Portugal
                [7 ]Institute of Research and Advanced Training in Health Sciences and Technologies (CESPU), Rua Central de Gandra, Gandra, PRD, Portugal
                Article
                10.1080/10408398.2021.1996327
                d58d60e6-4f79-4ce3-85ff-80d8114e390d
                © 2021
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