Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection

Derebe, M.G.; Zlatkov, Clare M; Gattu, Sureka; Ruhn, Kelly A.; Vaishnava, Shipra; Diehl, Gretchen E.; MacMillan, John B.; Williams, Noelle S.; Hooper, Lora V.

doi:10.7554/elife.03206

Cited by 114 publications

(165 citation statements)

References 51 publications

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“…S1 A and B). This structure differs from globular SAA1 and SAA3 proteins (18,19), which are significantly α-helical and devoid of β-sheet structure (Fig. S3C).…”

Section: Resultsmentioning

confidence: 88%

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits

Kollmer

Meinhardt

Haupt

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Electron tomography is an increasingly powerful method to study the detailed architecture of macromolecular complexes or cellular structures. Applied to amyloid deposits formed in a cell culture model of systemic amyloid A amyloidosis, we could determine the structural morphology of the fibrils directly in the deposit. The deposited fibrils are arranged in different networks, and depending on the relative fibril orientation, we can distinguish between fibril meshworks, fibril bundles, and amyloid stars. These networks are frequently infiltrated by vesicular lipid inclusions that may originate from the death of the amyloid-forming cells. Our data support the role of nonfibril components for constructing fibril deposits and provide structural views of different types of lipid-fibril interactions.aggregation | conformational disease | electron tomography | protein assembly | prion

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“…S1 A and B). This structure differs from globular SAA1 and SAA3 proteins (18,19), which are significantly α-helical and devoid of β-sheet structure (Fig. S3C).…”

Section: Resultsmentioning

confidence: 88%

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits

Kollmer

Meinhardt

Haupt

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…A recent study further showed that serum amyloid A binds and transports retinoids, which are induced in response to the infection (Dataset S3). Retinoids promote maturation of immune cells, elicit T H 17 responses, and facilitate the regeneration of damaged epithelial barriers (40,41). Coagulative activities.…”

Section: Resultsmentioning

confidence: 99%

Tissue dual RNA-seq allows fast discovery of infection-specific functions and riboregulators shaping host–pathogen transcriptomes

Nuss

Beckstette

Пименова

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

137

117

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Pathogenic bacteria need to rapidly adjust their virulence and fitness program to prevent eradication by the host. So far, underlying adaptation processes that drive pathogenesis have mostly been studied in vitro, neglecting the true complexity of host-induced stimuli acting on the invading pathogen. In this study, we developed an unbiased experimental approach that allows simultaneous monitoring of genome-wide infection-linked transcriptional alterations of the host and colonizing extracellular pathogens. Using this tool for Yersinia pseudotuberculosis-infected lymphatic tissues, we revealed numerous alterations of host transcripts associated with inflammatory and acute-phase responses, coagulative activities, and transition metal ion sequestration, highlighting that the immune response is dominated by infiltrating neutrophils and elicits a mixed T H 17/T H 1 response. In consequence, the pathogen's response is mainly directed to prevent phagocytic attacks. Yersinia up-regulates the gene and expression dose of the antiphagocytic type III secretion system (T3SS) and induces functions counteracting neutrophil-induced ion deprivation, radical stress, and nutritional restraints. Several conserved bacterial riboregulators were identified that impacted this response. The strongest influence on virulence was found for the loss of the carbon storage regulator (Csr) system, which is shown to be essential for the up-regulation of the T3SS on host cell contact. In summary, our established approach provides a powerful tool for the discovery of infection-specific stimuli, induced host and pathogen responses, and underlying regulatory processes.tissue dual RNA-seq | host-pathogen interaction | host-adapted metabolism | noncoding RNAs | Yersinia

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“…In addition to its putative role in immune response, SAA was proposed to modulate blood coagulation ( 11 ), monocyte and neturophil chemotaxis ( 12 ), and HDL functions in cholesterol transport and metabolism (13)(14)(15)(16). SAA is implicated in retinol transport ( 10 ), and elevated plasma SAA is a cardiovascular risk factor ( 17 ). Many aspects of normal functions of SAA and its pathological deposition in amyloid remain unclear and are intimately linked to HDL metabolism.…”

mentioning

confidence: 99%

Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL

Jayaraman

Haupt

Gursky

2015

Journal of Lipid Research

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Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection

Cited by 114 publications

References 51 publications

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits

Tissue dual RNA-seq allows fast discovery of infection-specific functions and riboregulators shaping host–pathogen transcriptomes

Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL

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