The human CD10 antigen is a single pass, type II transmembrane, 100&#x2009;kD cell surface glycoprotein belonging to peptidase M13 family. Identified in common acute lymphoblastic leukemia as a cancer specific antigen, CD10 is a cell surface ectoenzyme widely expressed on different types of cells. Earlier, it was used only as a cell surface marker to identify and differentiate between haematological malignancies. Later, reported to be present in various malignancies, it is thought to play significant role in cancer development and progression. Regulated expression of CD10 is necessary for angiogenesis and so forth. However its expression level is found to be deregulated in different cancers. In some cancers, it acts as tumor suppressor and inhibits tumor progression whereas in others it has tumor promoting tendency. However, its role in tumorigenesis remains unclear. This review summarises structural features, functions, and probable role of CD10 in cancer development.

Deepshikha Mishra

Sunita Singh

Gopeshwar Narayan

Role of B Cell Development Marker CD10 in Cancer Progression and Prognosis

The protein enhancer of rudimentary homolog, ERH, is a small, highly conserved protein that has been found in animals, plants, and protists. Genetic and biochemical interactions have implicated ERH in the regulation of pyrimidine biosynthesis, DNA replication, transcription, mRNA splicing, cellular proliferation, tumorigenesis, and the Notch signaling pathway. In vertebrates and insects, ERH is nuclearly localized; however, an examination of the ERH amino-acid sequence does not reveal any nuclear localization signals. In this paper we show that the first 24 amino acids contain sequences necessary and sufficient for nuclear localization. Through yeast two-hybrid screens, three new binding partners of ERH, RPS3, RPL19, and DDIT4, were identified. RPS3 was isolated from both human and Drosophila screens. These interactions suggest functions of ERH in cell growth, cancer, and DNA repair. The ERH sequences necessary for the interactions between ERH and RPS3 and RPL19 are mapped onto the same 24-amino-acid region in ERH which are necessary for nuclear localization, suggesting that ERH is localizing to the nucleus through binding to one of its DNA-binding partners, such as RPS3 or RPL19.

Stuart I. Tsubota

Anthony C. Phillips

Drosophila Enhancer of Rudimentary Homolog, ERH, Is a Binding Partner of RPS3, RPL19, and DDIT4, Suggesting a Mechanism for the Nuclear Localization of ERH

In mammals, tropomyosin is encoded by four known TPM genes (TPM1, TPM2, TPM3, and TPM4) each of which can generate a number of TPM isoforms via alternative splicing and/or using alternate promoters. In humans, the sarcomeric isoform(s) of each of the TPM genes, except for the TPM4, have been known for a long time. Recently, on the basis of computational analyses of the human genome sequence, the predicted sequence of TPM4<i>&#x3b1;</i> has been posted in GenBank. We designed primer-pairs for RT-PCR and showed the expression of the transcripts of TPM4<i>&#x3b1;</i> and a novel isoform TPM4<i>&#x3b4;</i> in human heart and skeletal muscle. qRT-PCR shows that the relative expression of TPM4<i>&#x3b1;</i> and TPM4<i>&#x3b4;</i> is higher in human cardiac muscle. Western blot analyses using CH1 monoclonal antibodies show the absence of the expression of TPM4<i>&#x3b4;</i> protein (&#x7e;28&#x2009;kDa) in human heart muscle. 2D western blot analyses with the same antibody show the expression of at least nine distinct tropomyosin molecules with a mass &#x7e;32&#x2009;kD and above in adult heart. By Mass spectrometry, we determined the amino acid sequences of the extracted proteins from these spots. Spot &#x201c;G&#x201d; reveals the putative expression of TPM4<i>&#x3b1;</i> along with TPM1<i>&#x3b1;</i> protein in human adult heart.

Dipak K. Dube

Syamalima Dube

Lynn Abbott

Ruham Alshiekh-Nasany

Charles Mitschow

Bernard J. Poiesz

Cloning, Sequencing, and the Expression of the Elusive Sarcomeric TPM4<i>&#x3b1;</i> Isoform in Humans

This study was done to assess the antifungal susceptibility of clinical isolates of<i> Candida albicans</i> and to evaluate its total protein profile based on morphological difference on drug resistance. Hundred and twenty clinical isolates of<i> C. albicans</i> from various clinical specimens were tested for susceptibility against four antifungal agents, namely, fluconazole, itraconazole, amphotericin B, and ketoconazole. A significant increase of drug resistance in clinical isolates of<i> C. albicans</i> was observed. The study showed 50&#x25; fluconazole and itraconazole resistance at 32&#x2009;<i>&#x3bc;</i>g&#x2009;mL<sup>&#x2212;1</sup> with a MIC<sub>50</sub> and MIC<sub>90</sub> values at 34 and 47 and 36 and 49&#x2009;<i>&#x3bc;</i>g&#x2009;mL<sup>&#x2212;1</sup>, respectively. All isolates were sensitive to amphotericin B and ketoconazole. The SDS-PAGE protein profile showed a prevalent band of &#x7e;52.5&#x2009;kDa, indicating overexpression of gene in 72&#x25; strains with fluconazole resistance. Since the opportunistic infections of<i> Candida</i> spp. are increasing along with drug resistance, the total protein profile will help in understanding the evolutionary changes in drug resistance and also to characterize them.

Kamal Uddin Zaidi

Abin Mani

Vijay Thawani

Arti Mehra

Total Protein Profile and Drug Resistance in <i>Candida albicans</i> Isolated from Clinical Samples

Ankyrin (ANK) repeat containing proteins are evolutionary conserved and have functions in crucial cellular processes like cell cycle regulation and signal transduction. In this study, through an entirely in silico approach using the first release of the moss genome annotation, we found that at least 54 ANK proteins are present in<i> P. patens</i>. Based on their differential domain composition, the identified ANK proteins were classified into nine subfamilies. Comparative analysis of the different subfamilies of ANK proteins revealed that<i> P. patens</i> contains almost all the known subgroups of ANK proteins found in the other angiosperm species except for the ones having the TPR domain. Phylogenetic analysis using full length protein sequences supported the subfamily classification where the members of the same subfamily almost always clustered together. Synonymous divergence (dS) and nonsynonymous divergence (dN) ratios showed positive selection for the ANK genes of<i> P. patens</i> which probably helped them to attain significant functional diversity during the course of evolution. Taken together, the data provided here can provide useful insights for future functional studies of the proteins from this superfamily as well as comparative studies of ANK proteins.

Niaz Mahmood

Nahid Tamanna

Analyses of<i> Physcomitrella patens</i> Ankyrin Repeat Proteins by Computational Approach

Commercially important<i> Commiphora</i> species are drought-tolerant plants and they are leafless for most of the year. Therefore, it is necessary to develop some molecular marker for the identification. Intended for that, in the present study, species-specific, sequence-characterized amplified regions (SCAR) markers were developed for proficient and precise identification of closely related species<i> Commiphora wightii</i> and<i> C. myrrha</i>, which may ensure the quality, safety, and efficacy of medicines made from these plants through adulterous mixing of these plants. Two species-specific RAPD amplicons were selected, gel-purified, cloned, and sequenced after screening of 20 RAPD primers. The sequence of 979 and 590 nucleotides (Genebank accession numbers K90051 and K90052) was used for development of 4 SCAR markers, namely, Sc1P, Sc1Pm, Sc2P, and Sc2Pm. Out of them, the Sc1Pm was specific for<i> C. wightii</i>, while Sc2P discriminated both the<i> Commiphora</i> species. These markers are first reported and will be useful for rapid identification of closely related<i> Commiphora wightii</i> and<i> C. myrrha</i> species.

Pramod Kumar Sairkar

Anjana Sharma

N. P. Shukla

SCAR Marker for Identification and Discrimination of <i>Commiphora wightii</i> and<i> C. myrrha</i>

This study was conducted to detect and characterize prevalent human group A rotavirus strains from 200 diarrheic children in Sokoto, Nigeria, by ELISA, monoclonal antibody (Mab) serotyping and Reverse Transcription-Polymerase Chain Reaction (RT-PCR) techniques. Rotavirus was detected in 25.5% of the children. The G-serotypes observed in circulation were G4: 16 (59.3%), G1: 4 (14.8%), G2: 3 (11.1%), G3: 3 (11.1%), and G12: 1 (3.7%). The monoclonal antibody (Mab) serotyping detected G1 and G3 but did not detect G4 and G2 serotypes. The Mab typing of the G1 and G3 serotypes was consistent with the result of the RT-PCR. The VP4 genotypes detected were P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M1" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><path id="g113-92" d="M290 -163V-135C183 -126 181 -122 181 -44V583C181 662 184 666 290 675V703H120V-163H290Z"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><path id="g113-55" d="M137 343C167 482 260 545 321 574C357 591 397 603 429 609L423 641C382 634 335 622 295 608C189 570 37 457 37 238C37 84 125 -12 242 -12C362 -12 447 89 447 209C447 311 374 393 267 393C247 393 226 386 204 376L137 343ZM227 337C318 337 361 256 361 173C361 105 336 22 258 22C176 22 126 120 126 240C126 266 127 291 132 310C155 323 189 337 227 337Z"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><path id="g113-94" d="M226 -163V703H56V676C162 667 165 662 165 584V-43C165 -122 162 -126 56 -136V-163H226Z"/></g></svg> 3 (13%), P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M2" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><path id="g113-57" d="M249 635C141 635 70 555 70 471C70 401 114 353 179 316C143 294 106 267 90 252C68 231 45 202 45 157C45 50 130 -12 237 -12C322 -12 435 52 435 169C435 256 372 304 303 343C349 374 375 398 383 407C401 429 411 458 411 487C411 569 344 635 249 635ZM238 603C285 603 337 567 337 482C337 422 310 385 276 358C205 393 145 426 145 500C145 552 179 603 238 603ZM248 20C183 20 125 70 125 163C125 218 158 268 206 300C284 261 355 217 355 143C355 66 308 20 248 20Z"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 11 (47.8%), and the rare human P genotype (P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M3" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><path id="g113-58" d="M244 635C114 635 38 519 38 422C38 317 111 240 217 240C236 240 255 244 277 256L345 292C311 140 203 39 59 15L64 -15C89 -15 150 -5 204 17C339 72 440 202 440 386C440 521 368 635 244 635ZM228 602C326 602 352 479 352 390C352 370 351 347 348 324C327 308 293 296 258 296C174 296 124 369 124 458C124 517 152 602 228 602Z"/></g><g transform="matrix(.013,0,0,-0.013,10.726,0)"><use xlink:href="#g113-94"/></g></svg>), found in 9 patients (39.1%). Nine strains identified with the common G and P combinations were G4 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M4" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-57"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 5 (56%), G4 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M5" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-55"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 1 (11%), G1 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M6" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-57"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 2 (22%), and G3 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M7" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-57"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 1 (11%), while seven strains with unusual combinations or rare G or P genotypes identified were G12 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M8" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-57"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 1 (14%), G2 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M9" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-57"/></g><g transform="matrix(.013,0,0,-0.013,10.725,0)"><use xlink:href="#g113-94"/></g></svg> 2 (29%), and G4 P<svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-2.15067pt" id="M10" height="11.439pt" version="1.1" viewBox="-0.0498162 -9.28833 15.3667 11.439" width="15.3667pt"><g transform="matrix(.013,0,0,-0.013,0,0)"><use xlink:href="#g113-92"/></g><g transform="matrix(.013,0,0,-0.013,4.485,0)"><use xlink:href="#g113-58"/></g><g transform="matrix(.013,0,0,-0.013,10.726,0)"><use xlink:href="#g113-94"/></g></svg> 4 (57%). To our knowledge this is the first molecular study of human rotavirus and report of rare human G and P serotypes in Sokoto State.

B. R. Alkali

A. I. Daneji

A. A. Magaji

L. S. Bilbis

F. Bande

Molecular Characterization of Human Rotavirus from Children with Diarrhoeal Disease in Sokoto State, Nigeria

Bacillus anthracis secretory protein protective antigen (PA) is primary candidate for subunit vaccine against anthrax. Attempts to obtain large quantity of PA from<i> Escherichia coli</i> expression system often result in the formation of insoluble inclusion bodies. Therefore, it is always better to produce recombinant proteins in a soluble form. In the present study, we have obtained biologically active recombinant PA in small scale<i> E. coli</i> shake culture system using three different expression constructs. The PA gene was cloned in expression vectors bearing trc, T5, and T7 promoters and transformed into their respective<i> E. coli</i> hosts. The growth conditions were optimized to obtain maximum expression of PA in soluble form. The expression construct PA-pET32c in DE3-pLysS<i> E. coli</i> host resulted in a maximum production of soluble PA (15&#x2009;mg&#x2009;L<sup>&#x2212;1</sup>) compared to other combinations. Purified PA was subjected to trypsin digestion and binding assay with lethal factor to confirm the protein&#x2019;s functionality. Biological activity was confirmed by cytotoxicity assay on J774.1 cells. Balb/c mice were immunized with PA and the immunogenicity was tested by ELISA and toxin neutralization assay. This study highlights the expression of soluble and biologically active recombinant PA in larger quantity using simpler<i> E. coli</i> production platform.

Nagendra Suryanarayana

Vanlalhmuaka

Bharti Mankere

Monika Verma

Kulanthaivel Thavachelvam

Urmil Tuteja

Soluble Expression and Characterization of Biologically Active<i> Bacillus anthracis</i> Protective Antigen in<i> Escherichia coli</i>

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