Structure of the Milk Fat Globule Membrane: New Scientific Advances Revealing the Role of Sphingomyelin in Topographical and Mechanical Heterogeneities

Lopez, Christelle

doi:10.1007/978-3-030-41661-4_3

Cited by 6 publications

(2 citation statements)

References 55 publications

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“…SM molecules are the most abundant sphingolipids naturally found in biological membranes where they have structural functions. The specific attractive molecular interactions between the NH group of SM and the OH group of cholesterol are preferentially involved in the formation of liquid-ordered lipid domains termed lipid rafts in cell membranes (Simons and Ikonen, 1997;Slotte, 2016), and in the MFGM (Lopez, 2020;Lopez et al, 2010). The specific chemical structure and physical properties of SM molecules are therefore prone to strong hydrogen bonding with OH-containing guest molecules in the bilayer membranes, which is not the case for glycerophospholipids including PC that do not contain the NH group (Slotte, 2016).…”

Section: Introductionmentioning

confidence: 99%

Solubilization of free β-sitosterol in milk sphingomyelin and polar lipid vesicles as carriers: Structural characterization of the membranes and sphingosome morphology

Lopez

David-Briand

Lollier

et al. 2023

Food Research International

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Section: Introductionmentioning

confidence: 99%

Solubilization of free β-sitosterol in milk sphingomyelin and polar lipid vesicles as carriers: Structural characterization of the membranes and sphingosome morphology

Lopez

David-Briand

Lollier

et al. 2023

Food Research International

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“…Milk fat globules are lipid droplets naturally secreted into milk by mammary epithelial cells (Lopez, 2020a) and comprise almost 98% of total raw milk fat (Lee et al, 2018). MFGs are composed of a triglyceride core surrounded by a biological membrane, called the milk fat globule membrane (MFGM), that is structured as a trilayer of polar lipids (phospholipids, sphingolipids, cholesterol) and membranespecific proteins (glycoproteins, enzymes) (Lopez, 2020b). A rich diversity of proteins and glycoproteins, called the MFGM proteins (MFGMPs), as well as glycolipids, are anchored in the outer layer of the MFGM and could act as ligands for bacteria or viruses (Spitsberg, 2005;Douëllou et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Serotype-dependent adhesion of Shiga toxin-producing Escherichia coli to bovine milk fat globule membrane proteins

et al. 2022

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Shiga toxin-producing Escherichia coli (STEC) are food-borne pathogens that can cause severe symptoms for humans. Raw milk products are often incriminated as vehicule for human STEC infection. However, raw milk naturally contains molecules, such as the milk fat globule membrane and associated proteins, that could inhibit pathogen adhesion by acting as mimetic ligands. This study aimed to: (i) evaluate the capability of STEC cells to adhere to bovine milk fat globule membrane proteins (MFGMPs), (ii) highlight STEC surface proteins associated with adhesion and (iii) evaluate the variation between different STEC serotypes. We evaluated the physicochemical interactions between STEC and milk fat globules (MFGs) by analyzing hydrophobic properties and measuring the ζ-potential. We used a plate adhesion assay to assess adhesion between MFGMPs and 15 Escherichia coli strains belonging to three key serotypes (O157:H7, O26:H11, and O103:H2). A relative quantitative proteomic approach was conducted by mass spectrometry to identify STEC surface proteins that may be involved in STEC-MFG adhesion. The majority of E. coli strains showed a hydrophilic profile. The ζ-potential values were between −3.7 and − 2.9 mV for the strains and between −12.2 ± 0.14 mV for MFGs. Our results suggest that non-specific interactions are not strongly involved in STEC-MFG association and that molecular bonds could form between STEC and MFGs. Plate adhesion assays showed a weak adhesion of O157:H7 E. coli strains to MFGMPs. In contrast, O26:H11 and O103:H2 serotypes attached more to MFGMPs. Relative quantitative proteomic analysis showed that the O26:H11 str. 21,765 differentially expressed five outer membrane-associated proteins or lipoproteins compared with the O157:H7 str. EDL933. This analysis also found strain-specific differentially expressed proteins, including four O26:H11 str. 21,765-specific proteins/lipoproteins and eight O103:H2 str. PMK5-specific proteins. For the first time, we demonstrated STEC adhesion to MFGMPs and discovered a serotype effect. Several outer membrane proteins—OmpC and homologous proteins, intimin, Type 1 Fimbriae, and AIDA-I—that may be involved in STEC-MFG adhesion were highlighted. More research on STEC’s ability to adhere to MFGMs in diverse biological environments, such as raw milk cheeses and the human gastrointestinal tract, is needed to confirm the anti-adhesion properties of the STEC-MFG complex.

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Application of atomic force microscopy for food foams and emulsions

Lopez

2023

Fundamentals and Application of Atomic Force Microscopy for Food Research

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Structure of the Milk Fat Globule Membrane: New Scientific Advances Revealing the Role of Sphingomyelin in Topographical and Mechanical Heterogeneities

Cited by 6 publications

References 55 publications

Solubilization of free β-sitosterol in milk sphingomyelin and polar lipid vesicles as carriers: Structural characterization of the membranes and sphingosome morphology

Solubilization of free β-sitosterol in milk sphingomyelin and polar lipid vesicles as carriers: Structural characterization of the membranes and sphingosome morphology

Serotype-dependent adhesion of Shiga toxin-producing Escherichia coli to bovine milk fat globule membrane proteins

Application of atomic force microscopy for food foams and emulsions

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