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Translocation of minerals from substrate to mushrooms can change the medicinal characteristics, commercial value, and biological efficiency of mushroom. In the present study, we demonstrated that addition of iron to the substrate reduces the yield of Pleurotus ostreatus mushroom. The biological efficiency of the mushroom varied from 36.53% on the unsupplemented substrate to 2.08% for the substrate with 500 mg/kg iron added. The maximum iron concentration obtained for mushroom was 478.66 mg/kg (dry basis) and the maximum solubility in vitro was 293.70 mg/kg (dry basis). Iron translocation increased the ash and protein content, reduced antioxidant activity, and enhanced the aroma and flavor characteristics of the mushroom. However mushroom has higher amounts of iron than vegetables like collard greens, it is not feasible to use mushrooms as the only dietary source of iron. The study also indicated that because of more bioaccumulation of iron in mycelium than in the mushroom, mycelium and not mushroom, could be a better alternative as a non-animal iron source.

BACKGROUND: The antigens of the Colton blood group system, Co(a) and Co(b), are encoded by a single gene that produces the aquaporin-1 (AQP1) protein, a water channel-forming protein, and are characterized by a single nucleotide polymorphism (SNP). A healthy Caucasoid blood donor originally typed as Co(a-b-) with commercial anti-Co(b) typed Co(a-b+) when retested with another anti-Co(b). Retyped with two different molecular biology methods, the sample came out Co(a)/Co(b). With the aim of understanding these discrepancies, serological, cytometric and molecular biology tests were carried out. METHODS: Absorption/elution studies with propositus red cells and controls were performed. The region spanning exon 1 to exon 4 of the Colton gene was sequenced, and flow cytometry analyses were carried out. RESULTS: Absorption/elution studies showed the absence of Co(a) and a weak expression of Co(b). DNA sequencing confirmed a CT heterozygosity at nucleotide position 134 (i.e. Co(a)/Co(b)), and an additional heterozygous CT was found at position 112. The presence of the Co(b) allele that encodes for the Co(b) antigen was confirmed. The new allele has the base cytosine at nucleotide 134 (Co(a)), in cis with the new nucleotide 112T. The nucleotide substitution 112C>T causes a missense mutation leading to an amino acid change from proline (CCG) to serine (TCG) at codon 38. CONCLUSION: The substitution found at codon 38 results in a modified AQP1 protein which explains the Co(a-b+) phenotype and possibly the weak expression of Co(b).

BACKGROUND: Traditionally, blood group typing has been performed with serologic techniques, the classical method being the hemagglutination test. Serotyping, however, may present important limitations such as scarce availability of rare antisera, typing of recently transfused patients, and those with a positive direct antiglobulin test. Consequently, serologic tests are being complemented with molecular methods. The aim of this study was to develop a low-cost, high-throughput method for large-scale genotyping of red blood cells (RBCs). STUDY DESIGN AND METHODS: Single-nucleotide polymorphisms associated with some clinically important blood group antigens, as well as with certain rare blood antigens, were evaluated: Jk a /Jk b , Fy a /Fy b , S/s, K/k, Kp a /Kp b , Js a /Js b , Co a /Co b , and Lu a /Lu b . Polymerase chain reaction (PCR)-amplified targets were detected by direct hybridization to microspheres coupled to allele-specific oligonucleotides. Cutoff values for each genotype were established with phenotyped and/or genotyped samples. RESULTS: The method was validated with a blind panel of 92 blood donor samples. The results were fully concordant with those provided by hemagglutination assays and/or sequence-specific primer (SSP)-PCR. The method was subsequently evaluated with approximately 800 blood donor and patient samples. CONCLUSION: This study presents a flexible, quick, and economical method for complete genotyping of large donor cohorts for RBC alleles.

We describe here the isolation and the full-length sequence of the coding region of the HLA new variant at the HLA-A locus officially named A*68020102. This variant shows an 11 base pairs deletion within the 5' UTR region. The exon sequence is identical to that of A*6802 and the commercially available anti-A68 typing sera react with the antigen coded by the allele A*68020102. This variant was originally identified in two unrelated Caucasoid families because of discrepant HLA typing results between serology, Sequence Specific Oligonucleotide Probe (SSOP), and SBT. In fact, the A68 assigned by serology was undetectable with the molecular techniques. This has occurred because the deletion present in A*68020102 prevents specific amplification of HLA-A locus by some commercially available typing kits.

In this brief communication we report the characterization of two new HLA-B variants officially named HLA-B*0817 and HLA-B*1311. The HLA-B*0817 allele was identified in a Caucasoid male candidate for renal transplantation in the North Italy Transplant program. The nucleotidic sequence of exons 2, 3 and 4 of this novel allele is identical to that of HLA-B*0804 except for three point mutations in exon 2: from A to G at position 259, from C to G at position 261 and from G to A at position 302. These mutations are responsible for two aminoacidic substitutions [Asn (r) Glu, codon 63, and Ser (r) Asn, codon 77]. HLA-B*1311 was found in a volunteer donor belonging to National Marrow Donor Program®. This new variant is identical to that of HLA-B*1301 except for three nucleotide substitutions at positions 353, 355 and 369 leading to two aminoacidic variations from Ile to Thr at codon 94 and from Ile to Leu at codon 95 and a silent mutation at codon 99.

We describe here the sequences of 3 new HLA-DRB1 variants officially named DRB1*03:05:03, DRB1*11:10:02, and DRB1*14:86. These novel alleles have been detected in 3 Caucasoid individuals by sequence-based typing. The first and second alleles are the result of a silent mutation, which does not imply any amino acid change. The sequence of DRB1*14:86 exhibits a single nucleotide difference with the allele DRB1*14:01:01 at position 239.

Two novel human leucocyte antigen (HLA) class I alleles were characterized by means of sequencing-based typing techniques. HLA-A*310103 was identified in a cord blood unit from a Caucasoid individual. The sequence of this allele is identical to that of HLA-A*310102 except for a silent mutation in exon 3 at position 480 (G --> A). HLA-B*9531 was found in a Caucasoid female patient registered on the heart transplantation waiting list in the North Italy Transplant programme. This new variant differs from HLA-B*1503 at position 572 (G --> C) in exon 3. This nucleotide change leads to an amino acidic substitution at codon 167 from tryptophan to serine.

We describe the isolation and characterization of two novel HLA-DRB1*11 alleles, officially named DRB1*1161 and 110404. These two new variants were both identified in two Caucasoid individuals. The exon 2 sequence of DRB1*1161 is identical to that of DRB1*110101 except at codon 41, where a nucleotide substitution (GAC>AAC) is responsible for an amino-acidic change from Asp to Asn. The exon 2 sequence of the second novel allele described here, DRB1*110404, differs from that of DRB1*110401 only at codon 34 where the nucleotidic change CAA>CAG gives rise to a silent mutation.

Two novel human leucocyte antigen (HLA) class I alleles have been identified in two Italian individuals. HLA-B*27:07:02 is identical to HLA-B*27:07:01 except for a nucleotide substitution at position 846 (A->G) resulting in a silent mutation. HLA-B*35:206 differs from the most similar allele, HLA-B*35:08:01, because of a single base mutation at position 149 (G->C) causing an aminoacidic change at codon 26 from Gly to Ala.

Summary In this report, we describe the identification and sequencing of a novel HLA-DPB1 allele, found in an Italian haematological patient. This allele is identical to DPB1*17:01 except for a single nucleotide substitution (GACGAG) at position 57, which changes the encoded amino acid from Asp to Glu.

Summary Here we describe the molecular modelling of the new variant HLA-B*35:132. This allele shows one mismatch with B*35:01:01:01 in exon 3 at position 575 where a T is substituted by a C, which implies an amino acidic change from Leucine to Proline. This seems not to alter the molecular structure and not to compromise the HLA complex and T-cell receptor interaction.

We describe here the sequence and the molecular modeling of a new variant of HLA-A*32 allele officially named A*32:22. This novel allele has been detected in an Italian cord blood sample by sequence-based typing (SBT). The mutation (CAT →CGT), which has occurred at codon 151, at nucleotide position 524, implies an amino acidic change from Histidine to Arginine. Residue 151 is located on top of the molecule inside the region contacted by T cell receptor (TCR) and it is possibly involved in docking TCR. A positively charged residue is maintained on this position determining a slight change of electrostatic potential on the molecular surface. This suggests a limited functional relevance of the amino acid substitution encoded by A*32:22.

A novel allele, officially named B*18:80, was detected in a Caucasoid individual by polymerase chain reaction-sequence-specific primers and SBT. The new allele differs from B*18:01:01 at two nucleotidic positions in codon 24 at exon 2.

Summary We describe a novel HLA-B*51 allele detected by DNA direct sequencing. The sequence of this allele has been officially named B*51:78 as a confirmatory sequence. This new allele nucleotide sequence differs from HLA-B*51:01:01 for two point mutations in exon 2 where codons 79–80 change from CGG-ATC to CGC-ACC (p.Ile80Thr).

We describe here two novel DRB1 alleles, officially named *040405 and *1190. DRB1*040405 differs from DRB1*0404 for one point mutation at codon 72 with no coding changes. DRB1*1190 is identical to DRB1*110101 except for a nucleotide substitution at codon 24 which causes an aminoacidic mutation from valine to methionine. Over time we have been witnessing the identification of a great number of new HLA alleles. DRB1 allelic variability is mostly present in the second exon and more that 760 alleles have been so far identified. Here, we report the description of two novel DRB1 alleles, named *040405 and *1190, and identified in two Caucasoid subjects.

Summary Here, we describe the characterisation of a new allelic variant of HLA-B*57. The novel allele, HLA-B*5728N, was identified with sequence-based typing in a Caucasoid family. HLA-B*5728N, differs from HLA-B*5701 because of a nucleotide substitution at position 420 (C->G) resulting in a coding change from Tyrosine to a stop codon.

Summary We report the identification of a novel HLA-DRB1*04, officially named DRB1*0460. It was detected during performing HLA-DRB1 high resolution typing by DNA sequencing-based method. The exon 2 nucleotide sequence of DRB1*0460 is identical to that of DRB1*040301 except at codon 63 (AGCAAC), changing the encoded serine to asparagine.

Genotype and allele frequencies for STR loci D3S1358, vWA, FGA, D8S1179, D21S11, D18S51, D5S818, D13S317, D7S820 were investigated in 289 unrelated Italian Caucasian individuals from the North and South regions. After co-amplification by polymerase chain reaction, automatic DNA profiling of these nine STR loci was performed by ABI PRISM((R)) 310 DNA Genetic Analyzer. For each locus, statistical parameters for forensic and paternity purposes were then calculated; the combined power of discrimination and the combined power of exclusion of all nine loci were 0.9999999999917 and 0.99992 for the Northern population and 0.9999999999921 and 0.99991 for the Southern population.

Background Killer cell immunoglobulin-like receptors (KIRs) are a family of inhibitory and activatory receptors that are expressed by most natural killer (NK) cells. The KIR gene family is polymorphic: genomic diversity is achieved through differences in gene content and allelic polymorphism. The number of KIR loci has been reported to vary among individuals, resulting in different KIR haplotypes. In this study we report the genotypic structure of KIRs in 217 unrelated healthy Italian individuals from 22 immunogenetics laboratories, located in the northern, central and southern regions of Italy. Methods Two hundred and seventeen DNA samples were studied by a low resolution PCR-SSP kit designed to identify all KIR genes. Results All 17 KIR genes were observed in the population with different frequencies than other Caucasian and non-Caucasian populations; framework genes KIR3DL3, KIR3DP1, KIR2DL4 and KIR3DL2 were present in all individuals. Sixty-five different profiles were found in this Italian population study. Haplotype A remains the most prevalent and genotype 1, with a frequency of 28.5%, is the most commonly observed in the Italian population. Conclusion The Italian Caucasian population shows polymorphism of the KIR gene family like other Caucasian and non-Caucasian populations. Although 64 genotypes have been observed, genotype 1 remains the most frequent as already observed in other populations. Such knowledge of the KIR gene distribution in populations is very useful in the study of associations with diseases and in selection of donors for haploidentical bone marrow transplantation.

A new allele, officially named HLA-A*2626, has been detected in a blood sample belonging to a Caucasian subject human leucocyte antigen typed for Lombardy Region external proficiency-testing exercise. The DNA sequences of exons 2, 3 and 4 of this new allele are identical to those of HLA-A*2601 except at codon 259 of exon 4 (CCT-->CTT). This variation modifies the encoded protein from proline to leucine.

In this brief communication, we describe a novel human leukocyte antigen-B (HLA-B) allele (HLA-B*1819). This allele, found in an Italian Caucasian individual, differs from HLA-B*180101 by three nucleotide changes in exon 3. These mutations are located at positions 527, 538, and 539 where a T, a C, and a T are substituted respectively, by an A, a T, and a G, leading to three aminoacidic substitutions at codon 152 from Valine to Glutamic Acid (GTG-->GAG), at codon 155 from Histidine to Glutamine (CAC-->CAG), and at codon 156 from Cysteine to Tryptophan (TGT-->TGG).

Here, we have described the characterization of two novel human leukocyte antigen-B (HLA-B) alleles. The new alleles, HLA-B*0732 and HLA-B*5809, were identified in Italian Caucasian individuals. B*0732 differs from HLA-B*0708 by one nucleotidic change at position 412 (from G to A) in exon 3, leading to an amino acidic substitution from Asp (GAC) to Asn (AAC) at codon 114. The sequence of B*5809 is identical to that of HLA-B*5801, except for a point mutation at position 583 in exon 3, where a T is substituted by a C. This change leads to an amino acidic substitution from Tyr (TAC) to His (CAC) at codon 171.

BACKGROUND Subjects who underwent solid organ transplantation are at higher risk for a wide variety of cancers. METHODS The authors investigated the origin of cancer in a cohort of 2,526 patients followed up for 60.7 +/- 35.6 months after kidney transplantation between 1990 and 2000 in seven transplant centers. RESULTS One hundred four of them developed cancer. All subjects who developed solid cancer within 6 months after transplantation (n=10) and a group of subjects who developed solid cancer after 6 months posttransplant (n=10) were selected. Short tandem repeat analysis was performed on paraffin-embedded biopsy specimens of tumors and on both donor and recipient pretransplant peripheral blood. Biologic material was obtained in 17 of the 20 selected patients (85.0%). The analysis showed that 16 of 17 tumors were genetically identical to the recipient. CONCLUSIONS The authors' results suggest that donor transmission of solid cancer is an unlikely event in their population.

This brief communication describes a new HLA-B allele (HLA-B*5808) detected in an Italian white volunteer bone marrow donor. With serology, this subject was typed as HLA-B15,17, whereas with molecular biology B*15, B*51, B*52 and/or B*58 could be assigned. In order to clarify the results, direct and cloning sequencing of exons 2, 3 and 4 were carried out. This new allele is identical to HLA-B*5801 in exon 2 except for a silent point mutation at nucleotide 141 where a C is substituted by a T; exons 3 and 4 are typical of HLA-B*51, B*52 and B*78. The peculiar sequence of B*5808 could explain the discrepancy between the serological and molecular typing results.

In this brief communication we report the characterization of two new HLA-B variants officially named HLA-B*0817 and HLA-B*1311. The HLA-B*0817 allele was identified in a Caucasoid male candidate for renal transplantation in the North Italy Transplant program. The nucleotidic sequence of exons 2, 3 and 4 of this novel allele is identical to that of HLA-B*0804 except for three point mutations in exon 2: from A to G at position 259, from C to G at position 261 and from G to A at position 302. These mutations are responsible for two aminoacidic substitutions [Asn (r) Glu, codon 63, and Ser (r) Asn, codon 77]. HLA-B*1311 was found in a volunteer donor belonging to National Marrow Donor Program(R). This new variant is identical to that of HLA-B*1301 except for three nucleotide substitutions at positions 353, 355 and 369 leading to two aminoacidic variations from Ile to Thr at codon 94 and from Ile to Leu at codon 95 and a silent mutation at codon 99.

As efforts continue to improve the health of all US citizens, oral health must not be overlooked. Oral health is an integral part of overall health status and oral diseases are among the most prevalent of all health problems.To describe the oral health status and oral health behaviors of African Americans.The National Health and Nutrition Examination Survey (NHANES III) data set was used to examine a range of oral health indicators of African Americans with specific attention to demographic and geographic factors. The original data set consisted of 20,050 subjects, gathered through the use of complex, multi-stage, stratified and clustered sampling techniques. Only African Americans were included in this study which resulted in a sample of 5,616. Statistical analysis was conducted to allow the proper modeling of the complex, stratified, multistage survey design and sample weights of NHANES III.Sixty-two percent of respondents indicated that they only visit the dentist when needed and had no regular visitation schedule. Dental health was worse for those individuals who were poor, unemployed, and uninsured. Regional differences in dental care appeared with individuals living in the south reporting poorer dental health.The findings from this study are useful for identifying sociodemographic and geographic factors related to oral health status. The insights gained from this study illustrate the need for tailoring oral health promotion programmes and services to specific groups within the African American community because service utilisation and response patterns and perceptions may be different.

In this report we describe a new HLA-DRB1 allele, DRB1*1353, which was initially recognized by a discrepancy between the results obtained with polymerase chain reaction using sequence-specific oligonucleotide (PCR-SSO) and sequence-specific primers (PCR-SSP). Sequence-based typing revealed sequence differences with other known HLA-DRB1 alleles. DRB1*1353 is identical to DRB1*13011 except for two nucleotide substitutions at nucleotide 84 (C(r)G) and at nucleotide 140 (T(r)A). These differences give rise to two amino acid substitutions at codons 28 and 47 from Asp to Glu and from Phe to Tyr, respectively.

We report the identification of a novel DRB3*02 using sequence-based typing (SBT). This new allele, officially named DRB3*0217, was detected while performing HLA high resolution typing of a bone marrow recipient and his siblings. DNA sequencing demonstrated the presence of a nucleotide substitution in exon 2 at position 199 where a C was substituted by a T. This point mutation at codon 67 (CTC--TTC) has resulted in an amino acid substitution from Leucine to Phenylalanine.

Summary A new variant of HLA-DQB1*04:03 allele officially designated as HLA-DQB1*04:03:02 was detected in two unrelated Caucasoid individuals by polymerase chain reaction-sequence-specific primers and SBT. The new allele nucleotide sequence differs from HLA-DQB1*04:03:01 for a single silent point mutation in exon 2 at position 159, codon 21.

We report the identification of a novel DRB1*11 using sequence-based typing. This new allele, officially named DRB1*1139, was detected while performing HLA-DRB1 high-resolution typing of a volunteer bone marrow donor. DRB1*1139 is identical to DRB1*11011 except at codon 51 (ACG--AGG) changing the encoded Threonine to Arginine. The triplet AGG has never been found in any other DRB1 allele. In fact, with standard polymerase chain reaction (PCR) amplification with sequence specific primers, the presented allele would have been interpreted as DRB1*1101 (Note).

We report herein the identification of HLA-B*4902. This new allele was identified in a Caucasian individual serologically typed as B49. The allele codifying for this antigen was not clearly detectable with polymerase chain reaction using sequence-specific primers (PCR-SSP) because of an atypical amplification pattern. DNA sequencing demonstrated the presence of a new variant due to two nucleotide substitutions (from G to C and from T to C) in exon 2 at nucleotides 309 and 311 respectively. These substitutions would result in a silent mutation and in one amino acid substitution from Ile to Thr, respectively.

We describe the isolation and characterization of a novel HLA-A null allele, officially named A*0127N. The A*0127N exon 2, 3, and 4 nucleotide sequence is identical to that of A*010101 except at position 553, where a G is substituted by a T, resulting in a coding change in exon 3 (GAG>TAG) from Glu to the stop codon AMB. The mutation described is responsible for the premature ending of the translation.

We report here the exon 2 sequence of the novel HLA-DRB1*110403 which differs from DRB1*110401 by a single synonymous nucleotide substitution at codon 78, where TAC is substituted by TAT. The variant originally identified in a Caucasoid individual was confirmed by cloning and sequencing.

A new HLA-B allele, B*5615, has been identified in a Caucasian individual by sequence-based typing. This allele shows a sequence identical to that of HLA-B*5601 except for two nucleotide substitutions that cause a change from TTA to TAC at codon 116 and an amino acidic change from Leucine to Tyrosine in the mature protein.

We report the identification of a novel HLA-DRB1*11 using sequence-based typing. This new allele, officially named DRB1*1150, was detected while performing HLA-DRB1 high-resolution typing of a candidate for bone marrow transplantation. DRB1*1150 is identical to DRB1*1143 except at nucleotides 200 and 227, where a T is substituted by a C and a T by an A, respectively. These differences give rise to two amino acid substitutions at codons 38 (Val-->Ala) and 47 (Phe-->Tyr).

We report herein the identification of a new HLA-DRB1 allele, DRB1*0707. This new allele was seen in a volunteer bone marrow donor (ID#118069) belonging to the German bone marrow donor registry (DKMS). HLA-DRB1*0707 was detected while performing HLA-DRB1 high resolution typing by sequence based typing. This novel allele differs from DRB1*070101 by a single nucleotide substitution at position 163 (C-->T) in exon 2.

We report the identification of a novel DRB3*02 using sequence-based typing (SBT). This new allele, officially named DRB3*0217, was detected while performing HLA high resolution typing of a bone marrow recipient and his siblings. DNA sequencing demonstrated the presence of a nucleotide substitution in exon 2 at position 199 where a C was substituted by a T. This point mutation at codon 67 (CTC-->TTC) has resulted in an amino acid substitution from Leucine to Phenylalanine.

We report the identification of a novel DRB1*11 using sequence-based typing. This new allele, officially named DRB1*1139, was detected while performing HLA-DRB1 high-resolution typing of a volunteer bone marrow donor. DRB1*1139 is identical to DRB1*11011 except at codon 51 (ACG-->AGG) changing the encoded Threonine to Arginine. The triplet AGG has never been found in any other DRB1 allele. In fact, with standard polymerase chain reaction (PCR) amplification with sequence specific primers, the presented allele would have been interpreted as DRB1*1101 (Note).

We report herein the identification of HLA-B*4902. This new allele was identified in a Caucasian individual serologically typed as B49. The allele codifying for this antigen was not clearly detectable with polymerase chain reaction using sequence-specific primers (PCR-SSP) because of an atypical amplification pattern. DNA sequencing demonstrated the presence of a new variant due to two nucleotide substitutions (from G to C and from T to C) in exon 2 at nucleotides 309 and 311 respectively. These substitutions would result in a silent mutation and in one amino acid substitution from Ile to Thr, respectively (Note).

Sir: To date, several papers have been published dealing with the comparison of serological and molecular typing for HLA class I on cadaveric organ donors [1, 5,6] lymphocytes. These analyses unanimously demonstrated an impressive advantage of the DNA technology over serotyping to the point that it is practised routinely today by many laboratories. The above mentioned studies referred to serological typing data performed in many different centers participating in the Collaborative Transplant Study or involved a limited number of cases. We wanted to address the question of how often cadaver organ donors are mistyped in our setting, where all HLA typing tests are centralized in a unique laboratory. This question is more than academic, due to clinical and ethical implications. In a system like ours [8], where HLA matching is an important parameter for kidney allocation, errors in HLA typing can change the recipient selection and have a negative impact on the transplant outcome, especially in re-transplants and sensitized patients. With this aim, we repeated with DNA techniques HLA-A, B cytotoxicity tests of 340 cadaveric organ donors referred to the North Italy Table 1 HLA-A,B determinations discrepant with the 2 methodologies (serology/PCRSSOP). The discrepancies are underlined in bold