Particles mixed withFigure 8. Proposed model of MBL-mediated macropinocytosis of EBOV. MBL carbohydrate recognition domains (CRD) bind to highly glycosylated mucin-rich regions of EBOV GP and the MBL-virion complex is presented to the cell surface. Then MBL binds to cognate cellular receptors, such as C1QBP or calreticulin [6] via MBL collagenous stalks. In this manner, MBL concentrates virus at t
Pathways such as macropinocytosis which is the canonical pathway for EBOV entry. Our data indicate that MBL also mediates internalization of virus via macropinocytosis but suggests that MBL-mediated uptake preferentially utilizes microtubules compared with the canonical EBOV pathway which is dependent on both microtubules and actin. doi:10.1371/journal.pone.0060838.gcirculating C4 [88], we specula
Ge activity .500 U/mL (13/21 vs 1/ 14, p,0.005) compared with MBL2 O/O or O/A haplotypes (O refers to B,C or D alleles). (EPS) Figure S3 Endoglycosidases cleave N-linked glycans in HIV-EBOV GP. We preincubated HIV-EBOZ GP virion-like particles (12,000 pg/ml) with PNGase F or endo H (10,000 U/ml each) diluted in DMEM or with DMEM alone for 1 hour at 37uC. Viruses then underwent gel electrophoresis;
Ge activity .500 U/mL (13/21 vs 1/ 14, p,0.005) compared with MBL2 O/O or O/A haplotypes (O refers to B,C or D alleles). (EPS) Figure S3 Endoglycosidases cleave N-linked glycans in HIV-EBOV GP. We preincubated HIV-EBOZ GP virion-like particles (12,000 pg/ml) with PNGase F or endo H (10,000 U/ml each) diluted in DMEM or with DMEM alone for 1 hour at 37uC. Viruses then underwent gel electrophoresis;
Particles mixed withFigure 8. Proposed model of MBL-mediated macropinocytosis of EBOV. MBL carbohydrate recognition domains (CRD) bind to highly glycosylated mucin-rich regions of EBOV GP and the MBL-virion complex is presented to the cell surface. Then MBL binds to cognate cellular receptors, such as C1QBP or calreticulin [6] via MBL collagenous stalks. In this manner, MBL concentrates virus at t
Particles mixed withFigure 8. Proposed model of MBL-mediated macropinocytosis of EBOV. MBL carbohydrate recognition domains (CRD) bind to highly glycosylated mucin-rich regions of EBOV GP and the MBL-virion complex is presented to the cell surface. Then MBL binds to cognate cellular receptors, such as C1QBP or calreticulin [6] via MBL collagenous stalks. In this manner, MBL concentrates virus at t
Ge activity .500 U/mL (13/21 vs 1/ 14, p,0.005) compared with MBL2 O/O or O/A haplotypes (O refers to B,C or D alleles). (EPS) Figure S3 Endoglycosidases cleave N-linked glycans in HIV-EBOV GP. We preincubated HIV-EBOZ GP virion-like particles (12,000 pg/ml) with PNGase F or endo H (10,000 U/ml each) diluted in DMEM or with DMEM alone for 1 hour at 37uC. Viruses then underwent gel electrophoresis;
Ge activity .500 U/mL (13/21 vs 1/ 14, p,0.005) compared with MBL2 O/O or O/A haplotypes (O refers to B,C or D alleles). (EPS) Figure S3 Endoglycosidases cleave N-linked glycans in HIV-EBOV GP. We preincubated HIV-EBOZ GP virion-like particles (12,000 pg/ml) with PNGase F or endo H (10,000 U/ml each) diluted in DMEM or with DMEM alone for 1 hour at 37uC. Viruses then underwent gel electrophoresis;