biostudies-literatureUnknown10Ning M<i>Spiroplasma eriocheiris</i> is a crustacean pathogen, without a cell wall, that causes enormous economic loss. <i>Macrobrachium rosenbergii</i> hemocytes are the major targets during <i>S. eriocheiris</i> infection. As wall-less bacteria, <i>S. eriocheiris</i>, its membrane protein should interact with host membrane protein directly and firstly when invaded in host cell. In this investigation, six potential hemocyte receptor proteins were identified firstly that mediate interaction between <i>S. eriocheiris</i> and <i>M. rosenbergii</i>. Among these proteins, lipopolysaccharide and β-1, 3-glucan binding protein (MrLGBP) demonstrated to bind to <i>S. eriocheiris</i> using bacterial binding assays and confocal microscopy. Four spiroplasma ligand proteins for MrLGBP were isolated and identFrontiers in immunology1852https://www.ebi.ac.uk/biostudies/studies/S-EPMC6694788biostudies-literature<i>Spiroplasma eriocheiris</i> Invasion Into <i>Macrobrachium rosenbergii</i> Hemocytes Is Mediated by Pathogen Enolase and Host Lipopolysaccharide and β-1, 3-Glucan Binding Protein.PMC6694788Hou LNing MXiu YMeng QGu WWang WYuan MBi Jfalse<i>Spiroplasma eriocheiris</i> Invasion Into <i>Macrobrachium rosenbergii</i> Hemocytes Is Mediated by Pathogen Enolase and Host Lipopolysaccharide and β-1, 3-Glucan Binding Protein.<i>Spiroplasma eriocheiris</i> is a crustacean pathogen, without a cell wall, that causes enormous economic loss. <i>Macrobrachium rosenbergii</i> hemocytes are the major targets during <i>S. eriocheiris</i> infection. As wall-less bacteria, <i>S. eriocheiris</i>, its membrane protein should interact with host membrane protein directly and firstly when invaded in host cell. In this investigation, six potential hemocyte receptor proteins were identified firstly that mediate interaction between <i>S. eriocheiris</i> and <i>M. rosenbergii</i>. Among these proteins, lipopolysaccharide and β-1, 3-glucan binding protein (MrLGBP) demonstrated to bind to <i>S. eriocheiris</i> using bacterial binding assays and confocal microscopy. Four spiroplasma ligand proteins for MrLGBP were isolated and ident2019-01-01T00:00:00Z20192026-04-07T23:10:03.576Z2025-05-31T22:23:27.492ZS-EPMC66947883144024410.3389/fimmu.2019.01852