Introduction: This study aimed to determine the prevalence of malnutrition and factors influencing malnutrition among children aged five years and below in Serian District of Sarawak, a district where the majority of people are indigenous. Methods: Using a cross-sectional method, a total of 177 children were randomly selected and assessed, and their mothers or caregivers were interviewed. Data were collected using a pretested questionnaire; anthropometric measurements were also taken. Data were analysed using SPSS version 17.0. Results: The prevalence of underweight, stunting and wasting in children aged five years and below was 20.9%, 11.9% and 10.2% respectively. The results suggest that the significant factors contributing to underweight are birth weight, frequency of child visit to the clinic, and individual insecurity. Only age, when complementary diet was introduced, was found to be significantly associated with stunting. For wasting, individual insecurity, duration of family planning and met recommended protein intake per day were found to be significant factors. Conclusion: The prevalence of malnutrition in children 5 years and below in Serian District of Sarawak is high compared to state figures. The major contributing factors were found to be manifested at the individual and family level. There is a need for appropriate public health promotion and socioeconomic improvement interventions towards improving the nutritional status and health of children in Serian District.
Child Nutrition Disorders, Malnutrition ; Thinness

This study evaluates the effect of maternal age, birth weight and infant sex on two main UCB parameters for use and long-term cryopreservation: TNC and volume. Data from 1000 UCB units were collected and analyzed in this study. The results indicate that TNC is correlated to infant birth weight and sex but not maternal age at delivery. Volume is only correlated to birth weight but not maternal age and infant sex.

We report an adult case of pontine infarct complicated by a community-acquired pneumococcal ventriculitis. An 85-year-old woman was referred to the hospital with left-sided weakness and persistent fever despite antibiotics therapy. Diffusion weight magnetic resonance image revealed high signal intensity on the right paramedian pontine and the occipital horn of the lateral ventricle. In the cerebrospinal fluid (CSF) examination, white blood cell count was 2,720 /mm3, glucose level was 4 mg/dL (simultaneous blood glucose level was 135 mg/dL), and CSF protein level was 2,025.4 mg/dL. On admission day 4, CSF culture showed Streptococcus pneumoniae. Despite continuous antibiotics treatment, she expired on admission day 7. In patients with pneumococcal ventriculitis, despite high mortality as in this case, early detection and treatment improve clinical outcome. Also aggressive treatment (intraventricular antibiotics injection, and pus drainage) should be considered.
Adult ; Aged, 80 and over ; Animals ; Anti-Bacterial Agents ; Blood Glucose ; Brain Stem ; Brain Stem Infarctions ; Cerebral Ventriculitis ; Diffusion ; Female ; Fever ; Glucose ; Horns ; Humans ; Lateral Ventricles ; Leukocyte Count ; Magnetic Resonance Spectroscopy ; Meningitis, Bacterial ; Streptococcus pneumoniae ; Suppuration

Nanobodies derived from camelids and sharks offer unique advantages in therapeutic applications due to their ability to bind to epitopes that were previously inaccessible. Traditional methods of nanobody development face challenges such as ethical concerns and antigen toxicity. Our study presents a synthetic, phagedisplayed nanobody library using trinucleotide-directed mutagenesis technology, which allows precise amino acid composition in complementarity-determining regions (CDRs), with a focus on CDR3 diversity. This approach avoids common problems such as frameshift mutations and stop codon insertions associated with other synthetic antibody library construction methods. By analyzing FDA-approved nanobodies and Protein Data Bank sequences, we designed sub-libraries with different CDR3 lengths and introduced amino acid substitutions to improve solubility. The validation of our library through the successful isolation of nanobodies against targets such as PD-1, ATXN1 and STAT3 demonstrates a versatile and ethical platform for the development of high specificity and affinity nanobodies and represents a significant advance in biotechnology.

Nanobodies derived from camelids and sharks offer unique advantages in therapeutic applications due to their ability to bind to epitopes that were previously inaccessible. Traditional methods of nanobody development face challenges such as ethical concerns and antigen toxicity. Our study presents a synthetic, phagedisplayed nanobody library using trinucleotide-directed mutagenesis technology, which allows precise amino acid composition in complementarity-determining regions (CDRs), with a focus on CDR3 diversity. This approach avoids common problems such as frameshift mutations and stop codon insertions associated with other synthetic antibody library construction methods. By analyzing FDA-approved nanobodies and Protein Data Bank sequences, we designed sub-libraries with different CDR3 lengths and introduced amino acid substitutions to improve solubility. The validation of our library through the successful isolation of nanobodies against targets such as PD-1, ATXN1 and STAT3 demonstrates a versatile and ethical platform for the development of high specificity and affinity nanobodies and represents a significant advance in biotechnology.

Nanobodies derived from camelids and sharks offer unique advantages in therapeutic applications due to their ability to bind to epitopes that were previously inaccessible. Traditional methods of nanobody development face challenges such as ethical concerns and antigen toxicity. Our study presents a synthetic, phagedisplayed nanobody library using trinucleotide-directed mutagenesis technology, which allows precise amino acid composition in complementarity-determining regions (CDRs), with a focus on CDR3 diversity. This approach avoids common problems such as frameshift mutations and stop codon insertions associated with other synthetic antibody library construction methods. By analyzing FDA-approved nanobodies and Protein Data Bank sequences, we designed sub-libraries with different CDR3 lengths and introduced amino acid substitutions to improve solubility. The validation of our library through the successful isolation of nanobodies against targets such as PD-1, ATXN1 and STAT3 demonstrates a versatile and ethical platform for the development of high specificity and affinity nanobodies and represents a significant advance in biotechnology.

Nanobodies derived from camelids and sharks offer unique advantages in therapeutic applications due to their ability to bind to epitopes that were previously inaccessible. Traditional methods of nanobody development face challenges such as ethical concerns and antigen toxicity. Our study presents a synthetic, phagedisplayed nanobody library using trinucleotide-directed mutagenesis technology, which allows precise amino acid composition in complementarity-determining regions (CDRs), with a focus on CDR3 diversity. This approach avoids common problems such as frameshift mutations and stop codon insertions associated with other synthetic antibody library construction methods. By analyzing FDA-approved nanobodies and Protein Data Bank sequences, we designed sub-libraries with different CDR3 lengths and introduced amino acid substitutions to improve solubility. The validation of our library through the successful isolation of nanobodies against targets such as PD-1, ATXN1 and STAT3 demonstrates a versatile and ethical platform for the development of high specificity and affinity nanobodies and represents a significant advance in biotechnology.

Nanobodies derived from camelids and sharks offer unique advantages in therapeutic applications due to their ability to bind to epitopes that were previously inaccessible. Traditional methods of nanobody development face challenges such as ethical concerns and antigen toxicity. Our study presents a synthetic, phagedisplayed nanobody library using trinucleotide-directed mutagenesis technology, which allows precise amino acid composition in complementarity-determining regions (CDRs), with a focus on CDR3 diversity. This approach avoids common problems such as frameshift mutations and stop codon insertions associated with other synthetic antibody library construction methods. By analyzing FDA-approved nanobodies and Protein Data Bank sequences, we designed sub-libraries with different CDR3 lengths and introduced amino acid substitutions to improve solubility. The validation of our library through the successful isolation of nanobodies against targets such as PD-1, ATXN1 and STAT3 demonstrates a versatile and ethical platform for the development of high specificity and affinity nanobodies and represents a significant advance in biotechnology.