Effects of MBL-associated serine protease-2 (MASP-2) on liquefaction and ulceration in rabbit skin model of tuberculosis. (October 2016)
- Record Type:
- Journal Article
- Title:
- Effects of MBL-associated serine protease-2 (MASP-2) on liquefaction and ulceration in rabbit skin model of tuberculosis. (October 2016)
- Main Title:
- Effects of MBL-associated serine protease-2 (MASP-2) on liquefaction and ulceration in rabbit skin model of tuberculosis
- Authors:
- Dong, Xinfang
Luo, Yanping
Gao, Qi
Lu, Xiaoling
Wang, Qian
Zhang, Yuan
Liu, Xun
Zhang, Lifeng
Wang, Jingqiu
Ma, Xingming
Zhu, Bingdong - Abstract:
- Abstract: Tuberculosis is a chronic infectious disease, which caused by Mycobacterium tuberculosis. It typically affects the functions of the lung and causes high morbidity and mortality rates worldwide. The lectin pathway, one of the complement cascade systems, provides the primary line of defense against invading pathogens. However, what is the specific effection between tuberculosis and complement is unknown. Mannose-binding lectin (MBL), a recognition subunit, binds to arrays of carbohydrates on the surfaces of pathogens, which results in the activation of MBL-associated serine protease-2 to trigger a downstream reaction cascade of complement system. The effects of human MBL-associated serine protease-2 (hMASP-2) were assessed in a rabbit-skin model by intradermal injection of 5 × 10 6 viable BCG bacilli. The rAd-hMASP-2 accelerated the formation of liquefaction and healing of the granuloma lesions, reduced the bacteria loads of the skin nodules. The serum levels of IL-2 and IFN-γ were significantly increasing during the granuloma and liquefaction phases in the rAd-hMASP-2 group. This study suggests that hMASP-2 can induce a protective efficacy in BCG-infected rabbit skin models, which affects both the progress of lesions and the survival of the mycobacteria within them. Highlights: The rabbit-skin model was establish by intradermal injection of viable BCG bacilli. The rAd-hMASP-2 accelerated the formation process of liquefaction and recovery. The rAd-hMASP-2 reduced theAbstract: Tuberculosis is a chronic infectious disease, which caused by Mycobacterium tuberculosis. It typically affects the functions of the lung and causes high morbidity and mortality rates worldwide. The lectin pathway, one of the complement cascade systems, provides the primary line of defense against invading pathogens. However, what is the specific effection between tuberculosis and complement is unknown. Mannose-binding lectin (MBL), a recognition subunit, binds to arrays of carbohydrates on the surfaces of pathogens, which results in the activation of MBL-associated serine protease-2 to trigger a downstream reaction cascade of complement system. The effects of human MBL-associated serine protease-2 (hMASP-2) were assessed in a rabbit-skin model by intradermal injection of 5 × 10 6 viable BCG bacilli. The rAd-hMASP-2 accelerated the formation of liquefaction and healing of the granuloma lesions, reduced the bacteria loads of the skin nodules. The serum levels of IL-2 and IFN-γ were significantly increasing during the granuloma and liquefaction phases in the rAd-hMASP-2 group. This study suggests that hMASP-2 can induce a protective efficacy in BCG-infected rabbit skin models, which affects both the progress of lesions and the survival of the mycobacteria within them. Highlights: The rabbit-skin model was establish by intradermal injection of viable BCG bacilli. The rAd-hMASP-2 accelerated the formation process of liquefaction and recovery. The rAd-hMASP-2 reduced the bacterial loads and increased serum levels of IL-2 and IFN-γ. … (more)
- Is Part Of:
- Microbial pathogenesis. Volume 99(2016)
- Journal:
- Microbial pathogenesis
- Issue:
- Volume 99(2016)
- Issue Display:
- Volume 99, Issue 2016 (2016)
- Year:
- 2016
- Volume:
- 99
- Issue:
- 2016
- Issue Sort Value:
- 2016-0099-2016-0000
- Page Start:
- 282
- Page End:
- 286
- Publication Date:
- 2016-10
- Subjects:
- Tuberculosis -- Complement -- MBL-associated serine protease-2 -- Rabbit
Pathogenic microorganisms -- Periodicals
Pathology, Molecular -- Periodicals
Communicable Diseases -- microbiology -- Periodicals
Communicable Diseases -- parasitology -- Periodicals
Micro-organismes pathogènes -- Périodiques
Pathologie moléculaire -- Périodiques
Electronic journals
616.9041 - Journal URLs:
- http://www.sciencedirect.com/science/journal/08824010 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=0882-4010;screen=info;ECOIP ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.micpath.2016.08.037 ↗
- Languages:
- English
- ISSNs:
- 0882-4010
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5756.955000
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