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Therefore, our hypothesis is that the prevalence of CCR5Δ32 allele would increase with advancing patient age.Thus, in order to investigate if the CCR5Δ32 polymorphism could confer a selective advantage on its carriers, we compared the frequencies of the CCR5Δ32 allele between two groups of SCD patients (pediatric and adult), seen at the Pernambuco Hematology and Hemotherapy Center, HEMOPE, in Northeastern Brazil, as well as the SCD adult group and a normal control group formed by blood donors.The patients were split into a pediatric group (3 months to 17 years old) with 483 individuals and an adult group (18 to 70 years old) with 312 individuals.An adult control group of 247 DNA samples from healthy blood donors (18 to 61 years old; 82.2% males) from the same geographical region and with ethnic background similar to those of the patients was analyzed for the CCR5Δ32 polymorphism.The amplified products were run on a 3% agarose gel stained with ethidium bromide and visualized under UV light. Amplification of the normal CCR5 allele produced a 206 bp fragment, while amplification of the mutant allele (CCR5Δ32) produced a 174 bp fragment.Figure 1: Agarose gel showing the CCR5 gene products in samples from a population of SCD patients in the state of Pernambuco.The mutation originated in Africa and is therefore more common in Brazilian populations where there is a greater proportion of individuals of African descent [6].

As the Th1 immune response is associated with inflammation, it has been proposed that the CCR5Δ32 allele could confer a selective advantage on patients with SCD because it induces a less efficient Th1 response [15].

It has been suggested that these episodes are associated with a chronic inflammatory condition with abnormal endothelial function involving interactions between the endothelium and sickle reticulocytes and white blood cells and thrombocytes.

SCD patients have elevated levels of inflammatory mediators, such as IL-6 and TNF-α, and adhesive molecules [9].

Sickle cell disease (SCD) is caused by either homozygosity for the hemoglobin S (Hb S) gene (sickle cell anemia, SCA) or compound heterozygosity for Hb S and another structural hemoglobin variant or beta-thalassemia [1, 2].

Hb S results from a single nucleotide substitution (GAG → GTG) at the sixth codon of the β-globin gene (HBB), which causes glutamic acid to be replaced by valine at the sixth position of the polypeptide chain [3–5].

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