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Dynamic niche-specific adaptations in Neisseria meningitidis during infection
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- Liu, Yan (author)
- Inner Mongolia Univ Nationalities, Sch Life Sci, Tongliao 028000, Peoples R China.
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- Zhang, Ding (author)
- Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut,Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, S-10691 Stockholm, Sweden.;Shanxi Agr Univ, Coll Anim Sci & Vet Med, Taigu 030801, Peoples R China.;Kitasato Univ, Grad Sch Infect Control Sci, Tokyo 1088641, Japan.
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- Engström, Åke (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Inner Mongolia Univ Nationalities, Sch Life Sci, Tongliao 028000, Peoples R China Institutionen för molekylär biovetenskap, Wenner-Grens institut (creator_code:org_t)
- Elsevier BV, 2016
- 2016
- English.
- In: Microbes and infection. - : Elsevier BV. - 1286-4579 .- 1769-714X. ; 18:2, s. 109-117
- Journal article (peer-reviewed)
Abstract
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- Neisseria meningitidis is an opportunistic human pathogen that usually colonizes the nasopharyngeal mucosa asymptomatically. Upon invasion into the blood and central nervous system, this bacterium triggers a fulminant inflammatory reaction with the manifestations of septicemia and meningitis, causing high morbidity and mortality. To reveal the bacterial adaptations to specific and dynamic host environments, we performed a comprehensive proteomic survey of N. meningitidis isolated from the nasal mucosa, CSF and blood of a mouse disease model. We could identify 51 proteins whose expression pattern has been changed during infection, many of which have not yet been characterized. The abundance of proteins was markedly lower in the bacteria isolated from the nasal mucosa compared to the bacteria from the blood and CSF, indicating that initiating adhesion is the harshest challenge for meningococci. The high abundance of the glutamate dehydrogenase (GdhA) and Opa1800 proteins in all bacterial isolates suggests their essential role in bacterial survival in vivo. To evaluate the biological relevance of our proteomic findings, four candidate proteins from representative functional groups, such as the bacterial chaperone GroEL, IMP dehydrogenase GuaB, and membrane proteins PilQ and NMC0101, were selected and their impact on bacterial fitness was investigated by mutagenesis assays. This study provides an integrated picture of bacterial niche-specific adaptations during consecutive infection processes.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Hälsovetenskap (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Health Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Infektionsmedicin (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Infectious Medicine (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Keyword
- Neisseria meningitidis
- Host adaptation
- Virulence
- Proteomic analysis
Publication and Content Type
- ref (subject category)
- art (subject category)
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