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Figure 3 | Virology Journal

Figure 3

From: Lassa virus-like particles displaying all major immunological determinants as a vaccine candidate for Lassa hemorrhagic fever

Figure 3

Lectin binding profiles on sucrose purified VLP. LASV Z+GPC+NP VLP fractions obtained from sucrose gradient sedimentation corresponding to those in Figure 1A were subjected to SDS-PAGE (3A) and lectin binding analysis on proteins transferred to nitrocellulose membranes (3B). A combination of agglutinins, GNA (Galanthus nivalis), SNA (Sambucus nigra), MAA (Maackia amurensis), PNA (Peanut), and DSA (Datura stramonium), were combined and used to probe VLP fractions 1 through 9 (3B, lanes 1 - 9). LASV NP, GP1, and GP2 generated in E. coli were used as unglycosylated protein controls (3B, lane 10). A combination of four glycoproteins was used as positive controls for lectin binding: carboxypeptidase Y (63 kDa), transferrin (80 kDa), fetuin (68, 65, 61 kDa), and asialofetuin (61, 55, 48 kDa) (3B, lane 11). For visual comparison purposes an SDS-PAGE gel was run with the same VLP fractions, stained with Coomassie BB-R250, and photographed (3A, lanes 1 - 9). LASV Z, Z+GPC+NP, Z+GPC, Z+NP VLP purified through 20% sucrose cushions were similarly analyzed for glycan binding (3C, lanes 1 - 4, respectively). The relative positions of GPC, GP1, and GP2 are noted to the left of the gel. Protein molecular weights in kDa are noted to the right of each image.

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