Efficacy and safety of the recombinant zoster vaccine: A systematic review and meta-analysis.

Unlabelled: In this systematic review with meta-analysis, the efficacy, effectiveness, and safety of the new GSK recombinant zoster vaccine (RZV) were assessed.Twenty three publications reporting on 14 studies were selected, including 2 pivotal RCTs in older immunocompetent adults (ZOE-50 and ZOE-70), 4 RCTs on immunocompromised patients (haematopoietic stem cell transplantation (HSCT), haematological malignancies, solid tumour, and renal transplantation), and 8 observational studies. Vaccine efficacy of RZV against herpes zoster (HZ) and postherpetic neuralgia (PHN) was very high in immunocompetent older adults (respectively 94% and 91.

Chronotropic incompetence is more frequent in obese adolescents and relates to systemic inflammation and exercise intolerance.

Background: Adults with obesity may display disturbed cardiac chronotropic responses during cardiopulmonary exercise testing, which relates to poor cardiometabolic health and an increased risk for adverse cardiovascular events. It is unknown whether cardiac chronotropic incompetence (CI) during maximal exercise is already present in obese adolescents and, if so, how that relates to cardiometabolic health.

Methods: Sixty-nine obese adolescents (body mass index standard deviation score = 2.

Comparison of flash glucose monitoring with real time continuous glucose monitoring in children and adolescents with type 1 diabetes treated with continuous subcutaneous insulin infusion.

Aims: In 2016 intermittently scanned continuous glucose monitoring (isCGM) became the first reimbursed CGM system in Belgium. Many children with type 1 diabetes (T1D) treated with multiple daily injections as well as with continuous subcutaneous insulin infusion (CSII) switched from self-monitoring of blood glucose to isCGM to monitor their treatment. In 2017 the Enlite® real-time CGM (rtCGM) system was reimbursed enabling its use with the Minimed® 640G insulin pump with integrated SmartGuard technology.

International clinical guidelines for the management of phosphomannomutase 2-congenital disorders of glycosylation: Diagnosis, treatment and follow up.

Phosphomannomutase 2 (PMM2-CDG) is the most common congenital disorder of N-glycosylation and is caused by a deficient PMM2 activity. The clinical presentation and the onset of PMM2-CDG vary among affected individuals ranging from a severe antenatal presentation with multisystem involvement to mild adulthood presentation limited to minor neurological involvement. Management of affected patients requires a multidisciplinary approach.

Evaluation of the FreeStyle® Libre Flash Glucose Monitoring System in Children and Adolescents with Type 1 Diabetes.

Background/aims: The FreeStyle® Libre Flash Glucose Monitoring System (FGM, Abbott) measures glucose concentrations in the interstitial fluid for up to 14 days. It has been approved for use in children aged > 4 years in January 2016. Experience in children is still limited.

PGM1 deficiency diagnosed during an endocrine work-up of low IGF-1 mediated growth failure.

Objective And Importance: Phosphoglucomutase 1 (PGM1) deficiency, first described as a glycogenosis (type XIV) is also a congenital disorder of glycosylation (CDG). We want to illustrate the wide clinical spectrum of PGM1 deficiency and in particular the associated disturbance in glucose metabolism and the endocrine dysfunction. Treatment with d-galactose is experimental.

TMEM165 deficiency causes a congenital disorder of glycosylation.

Protein glycosylation is a complex process that depends not only on the activities of several enzymes and transporters but also on a subtle balance between vesicular Golgi trafficking, compartmental pH, and ion homeostasis. Through a combination of autozygosity mapping and expression analysis in two siblings with an abnormal serum-transferrin isoelectric focusing test (type 2) and a peculiar skeletal phenotype with epiphyseal, metaphyseal, and diaphyseal dysplasia, we identified TMEM165 (also named TPARL) as a gene involved in congenital disorders of glycosylation (CDG). The affected individuals are homozygous for a deep intronic splice mutation in TMEM165.

A novel mutation causing mild, atypical fumarylacetoacetase deficiency (Tyrosinemia type I): a case report.

A male patient, born to unrelated Belgian parents, presented at 4 months with epistaxis, haematemesis and haematochezia. On physical examination he presented petechiae and haematomas, and a slightly enlarged liver. Serum transaminases were elevated to 5-10 times upper limit of normal, alkaline phosphatases were 1685 U/L (<720), total bilirubin was 2.

A new mutation in COG7 extends the spectrum of COG subunit deficiencies.

We describe a patient homozygous for a novel mutation in COG7, coding for one of the subunits of the Conserved Oligomeric Golgi complex, involved in retrograde vesicular trafficking. His brother showed a similar clinical syndrome and glycosylation defect but no DNA could be obtained from this patient. This mutation, c.

Identification of a novel PEX14 mutation in Zellweger syndrome.

Here we report a patient with Zellweger syndrome, who presented at the age of 3 months with icterus, dystrophy, axial hypotonia, and hepatomegaly. Abnormal findings of metabolic screening tests included hyperbilirubinaemia, hypoketotic dicarboxylic aciduria, increased C(26:0) and decreased C(22:0) plasma levels, and strongly reduced plasmalogen concentrations. In fibroblasts, both peroxisomal α- and β-oxidation were impaired.

Cerebrocostomandibular-like syndrome and a mutation in the conserved oligomeric Golgi complex, subunit 1.

We describe two patients with a cerebrocostomandibular-like syndrome and a novel mutation in conserved oligomeric Golgi (COG) subunit 1, one of the subunits of the conserved oligomeric Golgi complex. This hetero-octameric protein complex is involved in retrograde vesicular trafficking and glycosylation. We identified in both patients an intronic mutation, c.

Deficiencies in subunits of the Conserved Oligomeric Golgi (COG) complex define a novel group of Congenital Disorders of Glycosylation.

Processing of the glycan structures on glycoproteins by different glycosylation enzymes depends on, among other, the non-uniform distribution of these enzymes within the Golgi stacks. This compartmentalization is achieved by a balance between anterograde and retrograde vesicular trafficking. If the balance is disturbed, the glycosylation machinery is mislocalized, which can cause Congenital Disorders of Glycosylation type II (CDG-II), as illustrated by the identification of congenital defects in the Conserved Oligomeric Golgi (COG) complex in humans.

A common mutation in the COG7 gene with a consistent phenotype including microcephaly, adducted thumbs, growth retardation, VSD and episodes of hyperthermia.

We describe the clinical and biochemical characteristics in three patients from two different families diagnosed with Congenital Disorder of Glycosylation type IIe owing to a defect in Conserved Oligomeric Golgi complex (COG)7; one of the eight subunits of the COG. The siblings and an unrelated single child of consanguineous parents presented with growth retardation, progressive, severe microcephaly, hypotonia, adducted thumbs, feeding problems by gastrointestinal pseudo-obstruction, failure to thrive, cardiac anomalies, wrinkled skin and episodes of extreme hyperthermia. A combined disorder in the biosynthesis of N- and O-linked glycosylation with hyposialylation was detected.

A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation.

The hetero-octameric conserved oligomeric Golgi (COG) complex is essential for the structure/function of the Golgi apparatus through regulation of membrane trafficking. Here, we describe a patient with a mild form of a congenital disorder of glycosylation type II (CDG-II), which is caused by a homozygous nonsense mutation in the hCOG8 gene. This leads to a premature stop codon resulting in a truncated Cog8 subunit lacking the 76 C-terminal amino acids.