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1.
Fig. 5.

Fig. 5. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

Kinetics of NAb response to homologous viruses. Each group of 4 recently weaned pigs was separately inoculated with the indicated virus as described in Materials and Methods. The neutralizing activities of serum samples at the indicated time (in days) postinfection (PI) were measured against homologous virus (i.e., the same virus used for infection). Neutralization titers are expressed as means ± SEMs.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.
2.
Fig. 4.

Fig. 4. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

Effects of the absence of N-glycosylation sites in GP3 and GP5 on the in vitro growth properties. (A) Single-step growth curves of the indicated viruses upon infection of MARC-145 cells at an MOI of 5. Viral titers are expressed as means ± standard errors of the means (SEMs) (error bars) of data obtained from three independent experiments. (B) Plaque morphology in MARC-145 cells.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.
3.
Fig. 2.

Fig. 2. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

PRRSV-01 virus naturally lacks two N-glycosylation sites in its envelope glycoproteins. Multiple-sequence alignments of GP3 (A) and GP5 (B) collected from the NCBI database. Only regions that cover the potential N-linked glycosylation sites are shown. Asparagine (N) residues that contain the potential N-glycosylation sites are shown in boldface type. Positions in the PRRSV-01 sequence where the glycosylation sites are absent compared to other porcine reproductive and respiratory syndrome virus (PRRSV) strains are shown on a gray background.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.
4.
Fig. 6.

Fig. 6. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

Emergence of antibody escape mutant. (A) FL01-14dpi was isolated from a serum sample from a pig that had been infected with FL01 virus at 14 days postinfection (dpi). The neutralizing activities of serum samples from all four FL01-infected pigs at the indicated days postinfection (PI) were measured against FL01-14dpi. Neutralization titers are expressed as means ± SEMs. Kinetics of FL01 homologous antibody response was redrawn from Fig. 5 for comparison. (B) Mutations in the structural genes of FL01-14dpi compared to the corresponding genes of FL01 before infection. Amino acid changes that result in reappearance of N-glycosylation sites are shown in boldface type.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.
5.
Fig. 1.

Fig. 1. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

Neutralization phenotype of PRRSV-01. (A) Susceptibility of PRRSV-01 to cross-neutralization by heterologous antisera. The neutralizing activity of the indicated antiserum was separately measured against PRRSV-01 or against the homologous virus (i.e., the virus used for immunization to prepare each of the reference antisera). (B) Homologous neutralizing antibody (NAb) responses of pigs infected with PRRSV-01. Three recently weaned pigs (pigs 2533, 6180, and 7368) were inoculated with PRRSV-01 as described in Materials and Methods. Homologous neutralization titers of serum samples at the indicated time (in days) postinfection (PI) are shown. Neutralization titers were expressed as the reciprocal of the highest dilution that showed 90% or greater reduction in the number of fluorescent foci presenting in the control wells.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.
6.
Fig. 3.

Fig. 3. From: Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3.

(A) Schematic representations of the genomes of chimeric virus FL01 and mutants derived from it. The letter “Y” and the numbers below them represent potential N-glycosylation sites and their relative positions on the corresponding proteins. The absence of N-glycosylation sites at position 131 in GP3 and position 51 in GP5 is highlighted by rectangular boxes. N-glycosylation sites that are artificially reintroduced to the genome are shown with a lightning bolt symbol over the site. (B and C) Electrophoretic mobility of GP3 and GP5, respectively. MARC-145 cells were mock infected or infected with the indicated virus. At 36 h postinfection, proteins were radiolabeled as described in Materials and Methods and immunoprecipitated with anti-GP3 antibodies (B) or anti-GP5 antibodies (C). The immunoprecipitated proteins were left untreated (−) or were treated with PNGase F (+) and analyzed by electrophoresis on SDS-polyacrylamide gel. The approximate molecular masses (in kilodaltons) of the marker proteins are identified to the left of the gel. The positions of fully glycosylated proteins (black triangles) and of the protein species lacking one N-glycosylation site (white triangles) are shown to the right of the gel. Protein bands indentified by black arrows are the products of PNGase F digestion.

Hiep L. X. Vu, et al. J Virol. 2011 June;85(11):5555-5564.

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