Bovine herpesvirus type 1 (BoHV-1), a member of the Alphaherpesvirinae, causes a variety of diseases, which result in significant economic losses worldwide. Envelope glycoprotein D (gD) of BoHV-1 plays an important role in viral entry into the permissive cells, and protective immune response. The fine mapping epitope on the gD will contribute to the understanding of viral pathogenesis and development of alternative vaccines against various diseases associated with BoHV-1. We previously reported the preparation of a monoclonal antibody (MAb) 2B6, which was raised by a truncated recombinant gD protein, demonstrating a neutralizing activity against BoHV-1 infection in Madin–Darby bovine kidney cells. This study described the identification of a linear B-cell epitope on gD using MAb 2B6. A series of partially overlapping gD proteins with glutathione S-transferase tag were generated to define the epitope recognized by MAb 2B6. The amino acid (aa) sequence 323 GEPKPGPSPDADRPE 337 was recognized by MAb 2B6 using Western blot with the variedly truncated recombinant proteins. Importantly, this epitope was highly conserved among the typical members of BoHV-1, indicating that the epitope may be utilized in diagnosis of diseases due to BoHV-1 infection. Furthermore, the minimal linear epitope sequence 323 GEPKPGP 329 on gD recognized by MAb 2B6 was confirmed using single-aa residue deletion mutation in carboxyl terminal. This finding not only contributes to our understanding of gD of BoHV-1 virion but also shows a potential for the development of vaccine candidates and diagnostic techniques.
Bovine herpesvirus type 1 (BoHV-1) causes considerable economic losses to the cow industry. Vaccination remains an effective strategy to control the diseases associated with BoHV-1. However, live vaccines present safety concerns, especially in pregnant cows; thus, nonreplicating vaccines have been developed to control the disease. The envelope glycoproteins of BoHV-1 induce a protective immune response. In this work, selected epitopes on glycoproteins gD, gC, and gB were constructed in triplicate with linker peptides. Vaccination of rabbits demonstrated that P2-gD/gC/gB with AAYAAY induced higher specific antibodies than that with GGGGS linker. P2-gD/gC/gB with AAYAAY linker was fused with bovine interleukin-6 (BoIL-6) or rabbit IL-6 (RaIL-6) and bacterially expressed. Rabbits were intramuscularly immunized with 100 μg of P2-gD/gC/gB-BoIL-6, P2-gD/gC/gB-RaIL-6, P2-gD/gC/gB, P2-gD/gC/gB plus BoIL-6, P2-(gD-a)3-BoIL-6, or P2-(gD-a)3 emulsified with ISA 206 adjuvant thrice at 3-week intervals. P2-gD/gC/gB-BoIL-6 generated a higher titer of BoHV-1-specific antibodies, neutralizing antibodies, interferon (IFN)-γ, and IL-4 compared with P2-gD/gC/gB plus BoIL-6, P2-gD/gC/gB-RaIL-6, or other formulation. P2-gD/gC/gB-BoIL-6 triggered similar levels of antibodies and significantly higher titer of IFN-γ and IL-4 compared with inactivated bovine viral diarrhea (BVD)-infectious bovine rhinotracheitis (IBR) vaccine. Rabbits vaccinated with P2-gD/gC/gB-BoIL-6 dramatically reduced viral shedding and tissue lesions in lungs and trachea after viral challenge and reactivation compared with those with P2-gD/gC/gB plus BoIL-6 or P2-gD/gC/gB-RaIL-6. P2-gD/gC/gB-BoIL-6 provided protective effects against viral shedding and tissue pathogenesis similar to those of the inactivated vaccine. The data confirmed the safety and immunogenicity of multiple-epitope recombinant protein and a potential vaccine candidate to control the disease, especially for pregnant cattle.
High-quality remote sensing images play important roles in the development of ecological indicators’ mapping, urban-rural management, urban planning, and other fields. Compared with natural images, remote sensing images have more abundant land cover along with lower spatial resolutions. Given the embedded longitude and latitude information of remote sensing images, reference (Ref) images with similar scenes could be more accessible. However, existing traditional super-resolution (SR) approaches always depend on increases in network depth to improve performance, which limits the acquisition and application of high-quality remote sensing images. In this paper, we proposed a novel, reference-image-based, super-resolution method with feature compression module (FCSR) for remote sensing images to alleviate the above issue while effectively utilizing high-resolution (HR) information from Ref images. Specifically, we exploited a feature compression branch (FCB) to extract relevant features in feature detail matching with large measurements. This branch employed a feature compression module (FCM) to extract features from low-resolution (LR) and Ref images, which enabled texture transfer from different perspectives. To decrease the impact of environmental factors such as resolution, brightness and ambiguity disparities between the LR and Ref images, we designed a feature extraction encoder (FEE) to ensure accuracy in feature extraction in the feature acquisition branch. The experimental results demonstrate that the proposed FCSR achieves significant performance and visual quality compared to state-of-the-art SR methods. Explicitly, when compared with the best method, the average peak signal-to-noise ratio (PSNR) index on the three test sets is improved by 1.0877%, 0.8161%, 1.0296% , respectively, and the structural similarity (SSIM) index on four test sets is improved by 1.4764%, 1.4467%, 0.0882%, and 1.8371%, respectively. Simultaneously, FCSR obtains satisfactory visual details following qualitative evaluation.
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