Myelin basic protein in the cerebrospinal fluid of patients infected with HIV

Pfister, H.-W.; Einh�upl, K. M.; Wick, Manfred; Fateh‐Moghadam, A.; Huber, Michaela; Schielke, Eva; Goebel, F. D.; Matuschke, A.; Heinrich, B.; Bogner, Johannes R.; Fr�schl, M.; Pf�ffl, W.; Ackenheil, Manfred

doi:10.1007/bf00314458

Cited by 10 publications

(4 citation statements)

References 23 publications

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“…Studies on CSF PBM in CNS HIV infection are not common. It has been shown that participants with HIV encephalitis had mild to severe PBM levels (5–5.3 ng/mL) (Pfister et al 1989; Liuzzi et al 1992). In the present case, there was normalization of CSF PBM levels despite MRI demyelization.…”

Section: Discussionmentioning

confidence: 99%

Dynamic of CSF and serum biomarkers in HIV-1 subtype C encephalitis with CNS genetic compartmentalization—case study

et al. 2017

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Despite the effective suppression of viremia with antiretroviral (ARV) therapy, HIV can still replicate in the CNS. This was a longitudinal study of the CSF and serum dynamics of several biomarkers related to inflammation, the blood brain barrier, neuronal injury as well IgG intrathecal synthesis in serial samples of CSF and serum from a patient infected with HIV-1 subtype C with CNS compartmentalization. The phylogenetic analyses of plasma and CSF samples in an acute phase using next-generation-sequencing (NGS) and F-statistics analysis (FST), of C2-V3 haplotypes revealed distinct compartmentalized CSF viruses in paired CSF and peripheral blood mononuclear cell samples (PBMC). The CSF biomarker analysis in this patient showed that symptomatic CSF escape is accompanied by CNS inflammation, high levels of cell and humoral immune biomarkers, CNS barrier dysfunction and an increase in neuronal injury biomarkers with demyelization. Conclusions Independent and isolated HIV replication can occur in the CNS, even in HIV-1 subtype C, leading to compartmentalization and development of quasispecies distinct from the peripheral plasma. These immunological aspects of the HIV CNS escape have not been described previously. To our knowledge, this is the first report of CNS HIV escape and compartmentalization in HIV-1 subtype C.

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Section: Discussionmentioning

confidence: 99%

Dynamic of CSF and serum biomarkers in HIV-1 subtype C encephalitis with CNS genetic compartmentalization—case study

et al. 2017

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“…All these results suggest that the production of each Aβ species within brain cells and their clearance from the brain are differentially regulated. It is plausible that during physiological aging, these peptide levels in CSF are also altered according to the change in the level of the brain parenchymal Aβs, as CSF levels of molecules such as neuron-specific enolase, S-100 protein, myelin basic protein and glial fibrillary acidic protein reflect their concentration within the brain to a certain extent [29, 30, 31, 32]. Hence, the determination of those age-dependent alterations of Aβs in CSF may provide valuable information on mechanisms underlying their differential increase detected in vivo and in vitro and on its relevance to the pathogenesis for AD.…”

Section: Introductionmentioning

confidence: 99%

Age-Dependent Change in the Levels of Aβ40 and Aβ42 in Cerebrospinal Fluid from Control Subjects, and a Decrease in the Ratio of Aβ42 to Aβ40 Level in Cerebrospinal Fluid from Alzheimer’s Disease Patients

Fukuyama

Mizuno²,

Mori³

et al. 2000

Eur Neurol

101

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In order to address an age-dependent alteration in the concentration of β-amyloid polypeptides (Aβs) within the central nervous system and its probable predisposition to amyloidgenesis in Alzheimer’s disease (AD), we measured two species of soluble Aβs, Aβ40 and Aβ42, in cerebrospinal fluids (CSF) from randomly selected Japanese control subjects at various ages (n = 33) and then compared these data with those of probable Japanese AD patients (n = 23). CSF concentrations of Aβ40 and Aβ42 peptides were age-dependent (ANOVA, Bonferroni’s multiple comparison; p < 0.01 and p < 0.05, respectively) and were lower in the infant than in adults. From mid-20, the Aβ40 concentrations were decreasing while Aβ42 were rather stable. Aβs in CSF from AD patients (n = 23), whose ε4 allele frequency of the apolipoprotein E gene was higher than in controls (n = 83, p < 0.03), were not statistically different from those of age-matched controls (n = 13). A linear relationship was detected between the Aβ40 concentration and the Mini-Mental State Examination score (p < 0.05). The ratio of the Aβ42 to the Aβ40 level measured in the AD CSF samples was approximately 38% decreased compared to age-matched controls (p < 0.05). These data suggest that the physiological metabolism of soluble Aβs in the brain is regulated in an age-dependent manner, and that the ratio of Aβ42 to Aβ40 level in the CSF would be a useful marker for monitoring progression of AD.

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“…In the case of MBP, the antigenic region has been structurally characterized in complex with a major histocompatibility complex class 2 protein, and it assumes an extended conformation in the bound state [106,[235][236][237][238]. Molecular mimicry has been proposed as a mechanism for MBP-borne MS: the release of the antigenic epitope in the form of (auto)proteolytic peptides that resemble viral peptides can be detected by the immune system, which results in an attack against myelin and subsequent demyelination [23,228,233,[239][240][241]. While free disordered MBP is likely to be susceptible to degradation [229,[242][243][244], the recently described intermediate state in MBP-mediated membrane stacking could equally well be a target for proteolysis, especially since membrane stacking is dependent on the concentration of available MBP [24].…”

Section: Basic Proteins and Multiple Sclerosismentioning

confidence: 99%

Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease

Raasakka

Kursula

2020

Cells

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Myelin ensheathes selected axonal segments within the nervous system, resulting primarily in nerve impulse acceleration, as well as mechanical and trophic support for neurons. In the central and peripheral nervous systems, various proteins that contribute to the formation and stability of myelin are present, which also harbor pathophysiological roles in myelin disease. Many myelin proteins have common attributes, including small size, hydrophobic segments, multifunctionality, longevity, and regions of intrinsic disorder. With recent advances in protein biophysical characterization and bioinformatics, it has become evident that intrinsically disordered proteins (IDPs) are abundant in myelin, and their flexible nature enables multifunctionality. Here, we review known myelin IDPs, their conservation, molecular characteristics and functions, and their disease relevance, along with open questions and speculations. We place emphasis on classifying the molecular details of IDPs in myelin, and we correlate these with their various functions, including susceptibility to post-translational modifications, function in protein–protein and protein–membrane interactions, as well as their role as extended entropic chains. We discuss how myelin pathology can relate to IDPs and which molecular factors are potentially involved.

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Myelin basic protein in the cerebrospinal fluid of patients infected with HIV

Cited by 10 publications

References 23 publications

Dynamic of CSF and serum biomarkers in HIV-1 subtype C encephalitis with CNS genetic compartmentalization—case study

Dynamic of CSF and serum biomarkers in HIV-1 subtype C encephalitis with CNS genetic compartmentalization—case study

Age-Dependent Change in the Levels of Aβ40 and Aβ42 in Cerebrospinal Fluid from Control Subjects, and a Decrease in the Ratio of Aβ42 to Aβ40 Level in Cerebrospinal Fluid from Alzheimer’s Disease Patients

Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease

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