Pub Date : 2023-01-01Epub Date: 2023-05-17DOI: 10.1186/s44149-023-00080-0
Mingjun Su, Guanghui Zheng, Xiangwen Xu, Houhui Song
Coronaviruses are widespread in nature and can infect mammals and poultry, making them a public health concern. Globally, prevention and control of emerging and re-emerging animal coronaviruses is a great challenge. The mechanisms of virus-mediated immune responses have important implications for research on virus prevention and control. The antigenic epitope is a chemical group capable of stimulating the production of antibodies or sensitized lymphocytes, playing an important role in antiviral immune responses. Thus, it can shed light on the development of diagnostic methods and novel vaccines. Here, we have reviewed advances in animal coronavirus antigenic epitope research, aiming to provide a reference for the prevention and control of animal and human coronaviruses.
Supplementary information: The online version contains supplementary material available at 10.1186/s44149-023-00080-0.
{"title":"Antigen epitopes of animal coronaviruses: a mini-review.","authors":"Mingjun Su, Guanghui Zheng, Xiangwen Xu, Houhui Song","doi":"10.1186/s44149-023-00080-0","DOIUrl":"10.1186/s44149-023-00080-0","url":null,"abstract":"<p><p>Coronaviruses are widespread in nature and can infect mammals and poultry, making them a public health concern. Globally, prevention and control of emerging and re-emerging animal coronaviruses is a great challenge. The mechanisms of virus-mediated immune responses have important implications for research on virus prevention and control. The antigenic epitope is a chemical group capable of stimulating the production of antibodies or sensitized lymphocytes, playing an important role in antiviral immune responses. Thus, it can shed light on the development of diagnostic methods and novel vaccines. Here, we have reviewed advances in animal coronavirus antigenic epitope research, aiming to provide a reference for the prevention and control of animal and human coronaviruses.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1186/s44149-023-00080-0.</p>","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10189233/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9509468","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-01-01DOI: 10.1186/s44149-023-00075-x
Alexandria Zabiegala, Yunjeong Kim, Kyeong-Ok Chang
The spike protein (S) of SARS-CoV-2 is responsible for viral attachment and entry, thus a major factor for host susceptibility, tissue tropism, virulence and pathogenicity. The S is divided with S1 and S2 region, and the S1 contains the receptor-binding domain (RBD), while the S2 contains the hydrophobic fusion domain for the entry into the host cell. Numerous host proteases have been implicated in the activation of SARS-CoV-2 S through various cleavage sites. In this article, we review host proteases including furin, trypsin, transmembrane protease serine 2 (TMPRSS2) and cathepsins in the activation of SARS-CoV-2 S. Many betacoronaviruses including SARS-CoV-2 have polybasic residues at the S1/S2 site which is subjected to the cleavage by furin. The S1/S2 cleavage facilitates more assessable RBD to the receptor ACE2, and the binding triggers further conformational changes and exposure of the S2' site to proteases such as type II transmembrane serine proteases (TTPRs) including TMPRSS2. In the presence of TMPRSS2 on the target cells, SARS-CoV-2 can utilize a direct entry route by fusion of the viral envelope to the cellular membrane. In the absence of TMPRSS2, SARS-CoV-2 enter target cells via endosomes where multiple cathepsins cleave the S for the successful entry. Additional host proteases involved in the cleavage of the S were discussed. This article also includes roles of 3C-like protease inhibitors which have inhibitory activity against cathepsin L in the entry of SARS-CoV-2, and discussed the dual roles of such inhibitors in virus replication.
{"title":"Roles of host proteases in the entry of SARS-CoV-2.","authors":"Alexandria Zabiegala, Yunjeong Kim, Kyeong-Ok Chang","doi":"10.1186/s44149-023-00075-x","DOIUrl":"https://doi.org/10.1186/s44149-023-00075-x","url":null,"abstract":"<p><p>The spike protein (S) of SARS-CoV-2 is responsible for viral attachment and entry, thus a major factor for host susceptibility, tissue tropism, virulence and pathogenicity. The S is divided with S1 and S2 region, and the S1 contains the receptor-binding domain (RBD), while the S2 contains the hydrophobic fusion domain for the entry into the host cell. Numerous host proteases have been implicated in the activation of SARS-CoV-2 S through various cleavage sites. In this article, we review host proteases including furin, trypsin, transmembrane protease serine 2 (TMPRSS2) and cathepsins in the activation of SARS-CoV-2 S. Many betacoronaviruses including SARS-CoV-2 have polybasic residues at the S1/S2 site which is subjected to the cleavage by furin. The S1/S2 cleavage facilitates more assessable RBD to the receptor ACE2, and the binding triggers further conformational changes and exposure of the S2' site to proteases such as type II transmembrane serine proteases (TTPRs) including TMPRSS2. In the presence of TMPRSS2 on the target cells, SARS-CoV-2 can utilize a direct entry route by fusion of the viral envelope to the cellular membrane. In the absence of TMPRSS2, SARS-CoV-2 enter target cells <i>via</i> endosomes where multiple cathepsins cleave the S for the successful entry. Additional host proteases involved in the cleavage of the S were discussed. This article also includes roles of 3C-like protease inhibitors which have inhibitory activity against cathepsin L in the entry of SARS-CoV-2, and discussed the dual roles of such inhibitors in virus replication.</p>","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10125864/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10118413","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The cortex of the limb bones of chinchillas is very thin and brittle, so it is prone to fractures of the limb bones, among which fractures of the tibia, radius and ulna are the most frequent types. When a chinchilla has a closed fracture, it can be immobilized with a splint, cast, or bandage. If the broken end of the fracture pierces the skin, it is best to choose internal fixation or external fixation brackets for treatment. In this report, a 0.661 kg, 2-year-old male uncastrated chinchilla was presented to the Veterinary Teaching Hospital of Huazhong Agricultural University due to an old fracture of the right forearm. With the consent of the owner, we decided to use a 25-gauge needle as an IM pin to fix the fracture. Ten days after surgery, the wound had healed well, and the limb could support body weight, but the palm did not show a grasping position. Twenty four days after the operation, the affected limb had not regained the ability to grasp. The X-ray showed a slight rotation of the IM pin and good callus growth in the ulna, but not in the radius. One month after the operation, it was found that the function of the affected limb of the chinchilla was normal and the grasping ability was restored through follow-up consultation and the return visit.
{"title":"Case report: Diagnosis and treatment of a chinchilla's old radius and ulna fracture.","authors":"Siyu Long, YuJing Qiao, Hua Cao, Tiantian Qiu, Yuji Chen, Yaoqin Shen","doi":"10.1186/s44149-023-00072-0","DOIUrl":"https://doi.org/10.1186/s44149-023-00072-0","url":null,"abstract":"<p><p>The cortex of the limb bones of chinchillas is very thin and brittle, so it is prone to fractures of the limb bones, among which fractures of the tibia, radius and ulna are the most frequent types. When a chinchilla has a closed fracture, it can be immobilized with a splint, cast, or bandage. If the broken end of the fracture pierces the skin, it is best to choose internal fixation or external fixation brackets for treatment. In this report, a 0.661 kg, 2-year-old male uncastrated chinchilla was presented to the Veterinary Teaching Hospital of Huazhong Agricultural University due to an old fracture of the right forearm. With the consent of the owner, we decided to use a 25-gauge needle as an IM pin to fix the fracture. Ten days after surgery, the wound had healed well, and the limb could support body weight, but the palm did not show a grasping position. Twenty four days after the operation, the affected limb had not regained the ability to grasp. The X-ray showed a slight rotation of the IM pin and good callus growth in the ulna, but not in the radius. One month after the operation, it was found that the function of the affected limb of the chinchilla was normal and the grasping ability was restored through follow-up consultation and the return visit.</p>","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10033294/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9204617","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-12-12DOI: 10.1186/s44149-022-00062-8
Ying Xia, Siyu Long, Yuxuan Peng, S. Qin, Yaoqin Shen
{"title":"Isolation and identification of four pathogenic bacterial strains from edible snake (Elaphe carinata and Ptyas mucosus) farms with pneumonia in China","authors":"Ying Xia, Siyu Long, Yuxuan Peng, S. Qin, Yaoqin Shen","doi":"10.1186/s44149-022-00062-8","DOIUrl":"https://doi.org/10.1186/s44149-022-00062-8","url":null,"abstract":"","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44814370","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-12-01DOI: 10.1186/s44149-022-00063-7
Cuirong Wu, Lihui Liu, Yuxin Sui, Lulu Huang, Yang Chen, H. Hao, Yuanhu Pan, Zhenli Liu, Guyue Cheng
{"title":"Antimicrobial resistance and molecular typing of Salmonella in the chicken production chain in Hubei Province, China","authors":"Cuirong Wu, Lihui Liu, Yuxin Sui, Lulu Huang, Yang Chen, H. Hao, Yuanhu Pan, Zhenli Liu, Guyue Cheng","doi":"10.1186/s44149-022-00063-7","DOIUrl":"https://doi.org/10.1186/s44149-022-00063-7","url":null,"abstract":"","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47064394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-11-28DOI: 10.1186/s44149-022-00059-3
Haben Fesseha, Isayas Asefa
{"title":"Co-infection of fasciolosis and hydatidosis and their financial loss in cattle slaughtered at Wolaita Sodo municipal abattoir, southern Ethiopia","authors":"Haben Fesseha, Isayas Asefa","doi":"10.1186/s44149-022-00059-3","DOIUrl":"https://doi.org/10.1186/s44149-022-00059-3","url":null,"abstract":"","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-11-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45984757","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-10-17DOI: 10.1186/s44149-022-00056-6
Yu Wang, Yan Wang, Qingjie Peng, Zhijie Xiang, Yingyu Chen, Guiqiang Wang, Xijuan Wu, A. Guo, I. Robertson
{"title":"A case study investigating the effects of emergency vaccination with Brucella abortus A19 vaccine on a dairy farm undergoing an abortion outbreak in China","authors":"Yu Wang, Yan Wang, Qingjie Peng, Zhijie Xiang, Yingyu Chen, Guiqiang Wang, Xijuan Wu, A. Guo, I. Robertson","doi":"10.1186/s44149-022-00056-6","DOIUrl":"https://doi.org/10.1186/s44149-022-00056-6","url":null,"abstract":"","PeriodicalId":69105,"journal":{"name":"动物疾病(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44648913","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}