Entamoeba histolytica 5759 The amoeba can actually 'bore' into the intestinal wall, causing lesions and intestinal symptoms, and it may reach the blood stream. From there, it can reach different vital organs of the human body, usually the liver, but sometimes the lungs, brain, spleen, etc. A common outcome of this invasion of tissues is a liver abscess, which can be fatal if untreated. Ingested red blood cells are sometimes seen in the amoeba cell cytoplasm (Wiki: Entamoeba histolytica). Amoebiasis It has been shown that amoeba-specific sIgA antibodies are capable of blocking parasite adherence to target cells, preventing cytotoxic activity (Carrero et al., 2010). Other than infecting humans, mammals such as dogs and cats can become infected transiently, but are not thought to contribute significantly to transmission (Wiki: Entamoeba histolytica). Entamoeba histolytica is an anaerobic parasitic protozoan, part of the genus Entamoeba. Predominantly infecting humans and other primates, E. histolytica is estimated to infect about 50 million people worldwide. Many older textbooks state that 10% of the world population is infected, but these figures predate the recognition that at least 90% of these infections were due to a second species, E. dispar. Mammals such as dogs and cats can become infected transiently, but are not thought to contribute significantly to transmission. The active (trophozoite) stage exists only in the host and in fresh loose faeces; cysts survive outside the host in water, soils and on foods, especially under moist conditions on the latter. The cysts are readily killed by heat and by freezing temperatures, and survive for only a few months outside of the host. When cysts are swallowed they cause infections by excysting (releasing the trophozoite stage) in the digestive tract. The trophozoite stage is readily killed in the environment and cannot survive passage through the acidic stomach to cause infection. Symptoms can include fulminating dysentery, bloody diarrhea, weight loss, fatigue, abdominal pain, and amoeboma (Wiki: Entamoeba histolytica). Baboon Papio cynocephalus 9556 Bank vole Clethrionomys glareolus 447135 Bear Ursus americanus 9643 Birds Passeroidea 175121 Brown Trout Salmo trutta 8032 Buffalo Bison bison 9901 Carnivores Vulpes 9625 Cat Felis catus 9685 Catfishes Siluriformes 7995 Cattle Bos taurus 9913 Chicken Gallus gallus 9031 Chimpanzee Pan troglodytes 9598 chinchillas Chinchillidae 10150 Copper Pheasant Syrmaticus soemmerringii 9067 Deer Cervus elaphus 9860 Deer mouse Peromyscus maniculatus 10042 Dog Canis familiaris 9615 Ducks Anas 8835 Ferret Mustela putorius furo 9669 Fish Hyperotreti 117565 Gerbil Gerbillina 10045 Goat Capra hircus 9925 Gray wolf Canis lupus 9612 Guinea pig Cavia porcellus 10141 Hamster Mesocricetus auratus 10036 Horse Equus caballus 9796 Human Homo sapiens 9606 Macaque Macaca fascicularis 9541 Mongolian Gerbil Meriones unguiculatus 10047 Monkey Platyrrhini 9479 Mouse Mus musculus 10090 None None Parrot Psittacidae 9224 Pig Sus scrofa 9823 Rabbit Oryctolagus cuniculus 9986 Rainbow trout Oncorhynchus mykiss 8022 Rat Rattus 10114 Raven Corvus corax 56781 sei whale Balaenoptera borealis 9768 Sheep Ovis aries 9940 Squirrel Spermophilus richardsonii 37591 Tree shrew Tupaiidae 9393 Trouts, salmons & chars Salmoninae 504568 Turkey Meleagris gallopavo 9103 Vole Microtus ochrogaster 79684 Water buffalo Bubalus bubalis 391902 E. histolytica CEL-170/4 protein vaccine VO_0011414 Subunit vaccine Research Intraperitoneal injection (i.p.) Freund's incomplete and complete adjuvants Intraperitoneal injection (i.p.) E. histolytica alactose-specific adherence lectin heavy subunit (CEL-170/4) Recombinant protein preparation The galactose-specific lectin has been purified from a pathogenic strain of E. histolytica by monoclonal antibody affinity chromatography (Petri and Ravdin, 1991). Adult male gerbils were immunized by intraperitoneal or subcutaneous injection of 10 ,ug of the affinity-purified lectin emulsified in complete Freund's adjuvant (GIBCO, Grand Island, N.Y.) and boosted with 10 ,ug of the lectin in incomplete Freund's adjuvant at 2 and 4 weeks. Control gerbils were sham immunized with Freund's complete and incomplete adjuvants alone. Prechallenge gerbil sera were collected at 5 weeks after the initial immunization by cardiac puncture (Petri and Ravdin, 1991). Researcherse tested the ability of the galactose-specific adherence lectin of E. histolytica to elicit a protective immune response in conjunction with Freund's incomplete and complete adjuvants. Four independent trials demonstrated complete protection from amebic liver abscess formation in 67% of lectin-immunized gerbils. The gerbil antilectin antibodies were shown by Western immunoblotting to be directed to the heavy subunit (CEL-170/4) but not the light subunit of the lectin (Petri and Ravdin, 1991). Gerbils were challenged intrahepatically with E. histolytica (Petri and Ravdin, 1991). E. histolytica Eh29 protein vaccine VO_0011450 Subunit vaccine Research Intraperitoneal injection (i.p.) Incomplete Freund’s adjuvant Intraperitoneal injection (i.p.) E. histolytica alkyl hydroperoxide reductase Eh29 Recombinant protein preparation The full coding region of the gEh29 gene which encodes Eh29 (GenBank Accession No. X70996.1) was amplified by PCR and the 0.7 Kb amplicon was cloned into the expression vector pRSET-A (Invitrogen, CA, USA) following standard methods. After transformation into Escherichia coli BL21 (DE3) pLysS (Stratagene, CA, USA) positive clones were selected on ampicillin and chloramphenicol and were induced for expression of amino-terminal His-tagged Eh29 by incubation with 2 mM IPTG (Carrero et al., 2010). C3H/HeJ Mice were divided into seven groups of 10 animals. Two groups were left unimmunized. The remaining five groups were immunized using Eh29 combined with CT (Eh29 + CT), Eh29–CTxB fusion protein, CT alone, CTxB alone, or ARF combined with CT (ARF + CT). Mice were immunized orally with a dose of the relevant protein solution on days 1, 7, and 21 using a plastic cannula (standard wall spaghetti tubing; Chemplast Inc., USA). The protein solutions were prepared in 0.2 M NaHCO3, pH 8.3 such that one dose contained 100 μg of either recombinant Eh29, Eh29–CTxB or ARF, and 10 μg of commercial CT or CTxB, as pertinent. Additionally, on day 14, all immunized groups received an intraperitoneal boost with 25 μg of the corresponding recombinant protein emulsified in incomplete Freund’s adjuvant. The groups receiving only CT or CTxB were boosted with adjuvant emulsified in PBS (Carrero et al., 2010). 80% of C3H/HeJ mice immunized with Eh29 administered in combination with a subclinical dose of whole cholera toxin, but not as an Eh29-CTxB fusion, showed no evidence of infection in tissue sections harvested following intracecal challenge with virulent E. histolytica trophozoites. These results suggest that Eh29 is capable of inducing protective anti-amoebic immune responses in mice following oral immunization and could be used in the development of oral vaccines against amoebiasis (Carrero et al., 2010). On day 27 all mice (except those from one of the unimmunized groups) were infected intracecally with E. histolytica trophozoites recovered after three passages from hamster liver abscesses (Carrero et al., 2010). E. histolytica Gal/GalNAc lectin protein vaccine VO_0011451 Subunit vaccine Research Intraperitoneal injection (i.p.) Incomplete or complete Freund's adjuvant Intraperitoneal injection (i.p.) E. histolyica Gal/GalNAc lectin Recombinant protein preparation The native E. histolytica Gal/GalNAc lectin was purified from strain HM1:IMSS trophozoites grown under axenic conditions as described previously [5]. A large fragment of the Gal/GalNAc lectin heavy subunit spanning amino acids 578–1154 (“LecA”) was cloned into a pRSET-A vector (Invitrogen, Carlsbad, CA) with a kanamycin resistance gene and expressed in E. coli. The E. coli cells were lyzed by sonication and isolated inclusion bodies were denatured in inclusion body solubilization reagent (Pierce, Rockford, IL) (Houpt et al., 2004). C3H/HeJ Mice were immunized with a combined intranasal and intraperitoneal regimen over 6–9 weeks. Intranasal immunizations used 10 μg of antigen and 1 μg of cholera toxin (Sigma) administered intranasally in 20 μl of PBS into C3H mice under isoflurane anesthesia. Intraperitoneal immunizations used 15 μg of antigen emulsified in equal volumes of either complete (CFA) or incomplete Freund’s adjuvant (IFA) (Gibco, Grand Island, NY) injected via 20 gauge syringe. The lectin-1 trial utilized 150 μl of complete Freund’s adjuvant, the week 4 immunization of the lectin-2 trial two utilized 100 μl of CFA, and all other i.p. immunizations utilized 150 μl of incomplete Freund’s adjuvant. Sham-immunized mice from each trial were administered an identical regimen of PBS with adjuvant (Houpt et al., 2004). Vaccination prevented intestinal infection with efficacies of 84 and 100% in the two native lectin trials and 91 and 34% in the two LecA trials. Results show for the first time that immunization with the Gal/GalNAc lectin can prevent intestinal amebiasis in mice (Houpt et al., 2004). Mice were challenged intracecally with trophozoites 2 weeks after the final immunization (Houpt et al., 2004). E. histolytica SREHP protein vaccine VO_0011416 Subunit vaccine Research Oral Oral E. histolytica serine-rich protein (SREHP) Recombinant protein preparation Expressed the SREHP-MBP molecule in an attenuated vaccine strain of Salmonella typhimurium (Zhang and Stanley, 1996). female BALB/c mice or gerbils were deprived of water and food for 4 h and then were given 50 ml of 10% sodium bicarbonate solution per orogastric gavage with a 21-gauge ball-tipped gavage needle. Five minutes later, they received by gavage 50 ml of 0.16Mphosphate-buffered saline (PBS), pH 7.0, containing 109 S. typhimurium cells harboring either pSS3137 (Stm-SREHP) or pYA3137 (Stm-Ctrl). Mice and gerbils were immunized on days 0, 7, and 21. Serum samples were obtained on days 0, 7, 21, and 28 (Zhang and Stanley, 1996). Report describes a recombinant fusion protein containing the serine-rich Entamoeba histolytica protein (SREHP), a protective antigen derived from virulent amebae, and a bacterially derived maltose-binding protein (MBP) from an attenuated strain of Salmonella typhimurium. Gerbils vaccinated with S typhimurium SREHP-MBP were protected against amebic liver abscess after challenge with E. histolytica, the most common extraintestinal complication of amebiasis (Zhang and Stanley, 1996). On day 35 (14 days following the final booster immunization) control gerbils vaccinated with Stm-Ctrl and gerbils vaccinated with Stm-SREHP were challenged intrahepatically with 5 x 10^5 E. histolytica HM1:IMSS trophozoites (Zhang and Stanley, 1996). licensed Amoebiasis human vaccine Generic Unknown VO_0012171 Inactivated or "killed" vaccine Licensed A generic representation of vaccines utilized to prevent Amoebiasis infection in humans, typically employing inactivated Entamoeba histolytica organisms to elicit an immune response. These vaccines aim to reduce disease severity and incidence by providing immunity without the risk of live pathogen replication. CEL-170/4 Entamoeba histolytica VO_0011326 401088 5759 ? 170 kDa surface lectin 4.96 138236.38 1384 {ECO:0000269|PubMed:2000392, ECO:0000269|PubMed:2536731}. >sp|P23502.2|SL17_ENTHI RecName: Full=170 kDa surface lectin; Flags: Precursor MKLLLLNILLLCCLADKLNEFSADIDYYDLGIMSRGKNAGSWYHSYTHQYDVFYYLAMQPWRHFVWTTCE TTKGNKECYKYIINEDHNLNAQQLNNIKNLDKQDFCQKEYAYPIEKYEVDWDNVPVDEQQIESVDINGKT CFKYAAKRPLAYVYLNTKMTYATKTEAYDVCRMDFIGGRSITFRSFNNENKDFIDQYNTNTTSKCIIDVH KNNVNTHLAIILGITDSTVIKSLQENLSLLSQLKQSRVTLYYLKDDSYATDNIKLKDLKYETLVKYTAGQ GQVDPLVNQAKNDLFKMISDKKIKRGTMVVLMDNALGSEFNAETEFDRKNISVHTVVLNRNKDSKITYSA LKLVSLGPHYHEFTSNSEVSTTIDELFKGIRANLTERCDRDKCSGFCDAMNRCTCPMCCENDCFYTSCDV ETGSCIPWPKAKPKAKKECPATCVGLYECKDLEGCVVTKYNASCEPKVKCMVPYCDDDNNLKEVCKQKAN CEADQKPSSDGYCWSYTCDETTGFCKKYKHGNLCTGKTTNCQEYVCDSEQRCTVQEKVCVKTSPYIEMSC YVAKCNLNTGMCENRLSCDTYSSCGGDSTGSVCKCDASTGNQCKCNKVENGNYCDSSKHEICDYTGDKPK CIVSECTEDLVRDGCLIKRCNKTSKTTYWENVDCSNTKIEFAQDGKSETMCKPYYSATCLNGQCVVQAVG DVSNVGCGYCSMGTDNVITYHDDCDSRKSQCGNFNGKCQPNGDNSYSCVFEKDKTSSKSDNDICAECSSL TCPADTTYRTYTYDSKTGTCKATVKPTPSCSVCEKGKFVEKSKDQKLERKVTLEDGKEYQYNIPKDCVNE QCIPRTYVDCLANDDNFGEIYKFYLPCQAYVTATYHYSSLFNLTSYKLHLPQSEEFMKEADKEAYCTYEI TTRECKTCSLTETKEKVEEIDLCAEETKNGGVPFKCKNNNCIIDPNFDCQPIECKIQEIVITEKDGIKTT TCKDGTKTTCDTNNKRIEDARKAFIEGKEGIEQVECASTVCQNDNSCPIIADVEKCNQNTEVDYGCKAMT GECDGTTYLCKFVQLTDDPSLDSEHFRTKSGVELNNACLKYKCVESKGSDGKITHKWEIDTERSNIDPKP RNPCETATCDQTTGETIYTKKTCTVSEEFPTITPNQGRCFYCQCSYLDGSSVLTMYGETDKEYYDLDACG NCRVWNQTDRTQQLNNHTECILAGEINNVGAIAAATTVAVVVVAVVVALIVVSIGLFKTYQLVSSAMKNA ITTTNENAEYVGADNEATNAATYNG Protective antigen Researcherse tested the ability of the galactose-specific adherence lectin of E. histolytica to elicit a protective immune response in conjunction with Freund's incomplete and complete adjuvants. Four independent trials demonstrated complete protection from amebic liver abscess formation in 67% of lectin-immunized gerbils. The gerbil antilectin antibodies were shown by Western immunoblotting to be directed to the heavy subunit (CEL-170/4) but not the light subunit of the lectin [Ref1386:Petri and Ravdin, 1991]. Gal/GalNAc lectin Entamoeba histolytica HM-1:IMSS VO_0011323 3404842 67469085 EHI_046650 DS571321 XP_650534 294381 Unknown 16307 19930 - 4.63 126939.55 1207 transcript EHI_046650A >NW_001915036.1:16307-19930 Entamoeba histolytica HM-1:IMSS scf_1104750517013 genomic scaffold, whole genome shotgun sequence ATTATCCATTGAAATTAGCATTTGTGGCATTATCATCTTTAGCTGTGAATTGTGGGTTATTCACAGTATT ATCAACAGTATTCTTTCTTGCAGAAATAACAATATCAACAGTTTGCTTAATTCCAATAGCAATAATTACC ATAACAACAACAATTACTGCAACAACAACTGCAACAGTGGTACCAGCAGCAATAGCAGCTGTATTATCAA CGTCTTGCCATAACAAACAAACAGCATCTTTATCAACCAATTCATCATTGATCTTACAATTACCACATGC ATCTAATGAGAATCTATGATCTGCATAATCAGAGTACATTGTTAAAATCCACCCACTTTCAGATTGTAAT GAACATTCACAATAGAAACAATTCTTAGCTGCTTTAGACATATTAGGGAATTGAATATCAATATCACATT GAACAAAATTAGTTTCAATTTCTCCTGTTTCTTTGTCACAATAAGCGTCTTGACATTTATTCTTATAGAG CAATGCTTTTTCATGTCCATCAATATTACTTGTCCATTTATGTGTTATCACTCCTTCAGTGATAGTTTCA ACACAGGTATAATTATAACATTTATCAGTACAATCCCTATCATTAGATGGCTCATCACTACATTTTGTAA ATTCCTTCTTGATACAATATCCTGTACTTGTATCACATTTACCTGTTAATGAAGCACACCCAACATCAGC AGTATTTGATGAACAAATAGAATCATCATACACACCACTACATTTTGGAATACTTCCAGAAGCATCACAA TTAGTTTTCATACAAATAACTTCTCCAGGTTTACTAGGAGGAAGTGATGGACAAATAGTGACATTAGTTG GTTCACAAAGTTGGGATGTTCCAGTCTTTACTTGAATGAAACAATTATTAGTTGGATTACAATCTCCTTC ATATTTACAATCCCCATCTGAACAAGTCATCTGATAAATATTTCCAGATGCATCTACTTGATTTGGACAT TTATCAACAAGAGTAGACTCTTTATCCATTCCACTACAATACTTACATAAACTTTTTACCTTTTCTTCGT TTGAATTCCATTCACATTTATATTCATCAAATGTTGTGCCAATAATTAATTTGTAATCAAGAACATCAAG ACATTTACTAGGGAAATTCTCATGTTTAGTACAATCAAATTCATCATCAATATGACAACTTCCATCACGA CATACATATGGAATACCATTTATATTCTTTTTATTAGTACAATCCATTTTAATAAGTTTAGCTGGGTCAA CAAGAATATTATCATATGAACAATACATACACTGACTATCTAAAATAACTTTTGATCCATCTTTTACAAT AACTTTACATTCTCCATTTGCATATTCCCATTCATAATATTGTTCACAATCACTTAATCTATCTTTGAAA AGATCTTTACAATCATATTCATCTGGTGCTTGACATTCTCCATCTTTACAAACAAATGGAATTCCTTGTG ATGTAGTCAAACCTTCACATTTATTAACAATTTCATTTCCATCACAAATTTTACATTCTTGAATTGCTTT ATCTGTAGTTACAAGTATACATTCTCTATTTCCACTACATACATAATTAGCATATCCATCACATTTTTCA GGTACTTTTTCTTTACATACATATTCCTCTTGGTCTACAACATATTGAGTCGTTCCATTAGCAGTATATT CTTTACAGACTTTTTTGTAACAACCTTCCCAAACAATATCATGTCCTTTAAGCTCTTCACAATTATCAAC ATTAATACATTTTGGATCCCCATCTGTATAATCACAAACTTCGCCATTAGTACATCCATTACTAGTATCA CATTTACATTGATATGATGTAGATGCATCACATCGACAATTTCCATTAACTTTCCCACACACTTTCATTC CAGAACTACATCCAACTAAATTCATAACACAATTTCCAGTTTCACTATCACATGTAGCTTCATAACATGG ATTTTCTTCATATGGAGATACTTTAATACATTTCTTTTCTTGAACCATACATGTTCCAGCAGAACAATAA TATTCTTCACACTTACTTGATAATTTAGGACAATAGCTAGATGATTGTAATGTATTTGGAATACATTCTC CATTTGTTCTATCACATGAATAAGTTCTACAAACAAATTTTTCTACTCCAGATTCAATAATTGAAGATGG CTTAATATCATCAGTACAATTACTTCTAAAAGCACAGTTGTTTCCTGAACAATAAGGCTCTAAACATTTA ACTGTTGAAACACATTTATTTTGTTCAATAGTACATCCAATATCTTCAACACATTTAGCTACACCTAAAC AACTTTCTGTTGTACATTTTCTTTTTTCAATTTTATGATCAGCACTTGGATAATAAACACATTCTCCATT TTCAGTATTACATGTTGTATAATAACATTCACTATGACAACACATTGGACATGTACAACGAGCCCCACCA TCACAAAATCCTTTACAAGTTTTTCTATCACATAATTCAGTATTATTTGCCATAATAGTATTATATAATT GTGGAAGAGAAGTGCTTAATGATGAAACAGATGATTTAAAGTAATGTTCCCCTTTATTAACTAATTCTTC AAGTTGATATTCTTCTTCAATTGATGAGTCTAAATTAAATACATAAAATGTAGTATTATGACTATAAAGA GTATTTAACATATTAGAAGCTTTTCCTGCATATTTACTGATATAAACAATATTCTTTCCTGCTTTTGAAG ACATTTGGTTATATACAGTTTCTATAGCTTTTGTTTCATTTCCTTTTCTCATAACAGTAATTCCATTTAA TACATTTTTAATATTATCCTTTGTTACTAATGAATCTGAATGATATGGATTTTGAGAGTTAATATAATAA GCGAATGAAGTATCATTTGGGAATAAATCAATCAAATAATTAACAATTGAACTAAATATATTTCTTAATG TATTAGTCATATCTAAATTAACAACAATACCAACCGCCATATTATTTGTTGGTGGTAAAACAGTAGAAGC ATGACATTTAGTAATATTATTATTTTTATAGTCAGTGATAAAATTATCAGAAAATTCTGAACTACTTCTA AATGTAATAACTTTACCTCCAATATATTCAAATCTACATGGTGACATTCCTTCTGCATATTTATTTGTTA CATCATATGTTTTTTCAAGAAAATATGCAGCTGTTAATGGTGGTTTAGCAGCATATTTATAACAAGTTAA TCCATTAATTGAAACAACTGGTAATTTAGAAGTATCTGATGGAATACGAGACCAATCCAATTGATATTCT CTAATAGGATATCCCATTTTCTTTCTACACATATTTTCTTCTTTTGTATCACTTTTATCACGGTCATAAT CTTGATTAAATATCATTTCAGTAAAATATTTACTTTGGTCTTTAGTAGGAAAATTACTATCAATAGTTGT CCATTCTAAATTTCTCCATGGTTGCATTGTTAAATAATAAAATACACTATACTTTTTATTTACACTTCTT GACCATGAAGCTGCATTTTTACCCATTCCCATTCTTCCTTTATCTTGGATATCTACAGTTCCAGAAAACT CATTTAAATTAATTCCTAAAGCAATTGAAGCATAAAATAATACCAAAATTATCA >XP_650534.1 Gal/GalNAc lectin heavy subunit, putative [Entamoeba histolytica HM-1:IMSS] MIILVLFYASIALGINLNEFSGTVDIQDKGRMGMGKNAASWSRSVNKKYSVFYYLTMQPWRNLEWTTIDS NFPTKDQSKYFTEMIFNQDYDRDKSDTKEENMCRKKMGYPIREYQLDWSRIPSDTSKLPVVSINGLTCYK YAAKPPLTAAYFLEKTYDVTNKYAEGMSPCRFEYIGGKVITFRSSSEFSDNFITDYKNNNITKCHASTVL PPTNNMAVGIVVNLDMTNTLRNIFSSIVNYLIDLFPNDTSFAYYINSQNPYHSDSLVTKDNIKNVLNGIT VMRKGNETKAIETVYNQMSSKAGKNIVYISKYAGKASNMLNTLYSHNTTFYVFNLDSSIEEEYQLEELVN KGEHYFKSSVSSLSTSLPQLYNTIMANNTELCDRKTCKGFCDGGARCTCPMCCHSECYYTTCNTENGECV YYPSADHKIEKRKCTTESCLGVAKCVEDIGCTIEQNKCVSTVKCLEPYCSGNNCAFRSNCTDDIKPSSII ESGVEKFVCRTYSCDRTNGECIPNTLQSSSYCPKLSSKCEEYYCSAGTCMVQEKKCIKVSPYEENPCYEA TCDSETGNCVMNLVGCSSGMKVCGKVNGNCRCDASTSYQCKCDTSNGCTNGEVCDYTDGDPKCINVDNCE ELKGHDIVWEGCYKKVCKEYTANGTTQYVVDQEEYVCKEKVPEKCDGYANYVCSGNRECILVTTDKAIQE CKICDGNEIVNKCEGLTTSQGIPFVCKDGECQAPDEYDCKDLFKDRLSDCEQYYEWEYANGECKVIVKDG SKVILDSQCMYCSYDNILVDPAKLIKMDCTNKKNINGIPYVCRDGSCHIDDEFDCTKHENFPSKCLDVLD YKLIIGTTFDEYKCEWNSNEEKVKSLCKYCSGMDKESTLVDKCPNQVDASGNIYQMTCSDGDCKYEGDCN PTNNCFIQVKTGTSQLCEPTNVTICPSLPPSKPGEVICMKTNCDASGSIPKCSGVYDDSICSSNTADVGC ASLTGKCDTSTGYCIKKEFTKCSDEPSNDRDCTDKCYNYTCVETITEGVITHKWTSNIDGHEKALLYKNK CQDAYCDKETGEIETNFVQCDIDIQFPNMSKAAKNCFYCECSLQSESGWILTMYSDYADHRFSLDACGNC KINDELVDKDAVCLLWQDVDNTAAIAAGTTVAVVVAVIVVVMVIIAIGIKQTVDIVISARKNTVDNTVNN PQFTAKDDNATNANFNG Protective antigen Study tested if vaccination with the E. histolytica Gal/GalNAc lectin could prevent cecal infection in a C3H mouse model of amebic colitis. Vaccination prevented intestinal infection with efficacies of 84 and 100% in the two native lectin trials and 91 and 34% in the two LecA trials. Results show for the first time that immunization with the Gal/GalNAc lectin can prevent intestinal amebiasis in mice [Ref1383:Houpt et al., 2004]. gEh29 Entamoeba histolytica VO_0011322 399673 399674 CAA50324.1 CDD:223527 CDD:239313 GOA:P19476 InterPro:IPR000866 InterPro:IPR012335 InterPro:IPR012336 InterPro:IPR017936 InterPro:IPR019479 UniProtKB/Swiss-Prot:P19476 5759 ? alkyl hydroperoxide reductase 7.38 25237.95 304 Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]; COG0450 >gi|399673|emb|X70996.1| E.histolytica gEh29 gene for alkyl-hydroperoxidase reductase TTAGTTAAAAAGTATTTGATGACTTATTAGTTCATGTTACATATACAAAAATAATACTTTTATTGAAGTT TTGTGCCAATACATTTCTCTTTCTCCTCATCATATTCTTCATTAGATTCTTTGAGAATGTGTGGATGTGT GTATCTCCGTTTTCTTCTTTTTATCTAGTCATTTTTGTTTTCTATTTACCAGTTCTTTCATTATAAGTTG TTTAAATGTTGAATAATTACCATAATGAGAATAATGCAGAAGTGATGATGACGACATTTTTATTTTAGTT AAGTAAAGATGATTTTGGTAGTTCATTTGTCATTTAAACATCTCATCATCACCACAATCTCATCAATTCA ATCAGTCAAATGTCTTGCAATCAACAAAAAGAGTGTTGTAAAAAAGAATGTCAAGAGAAAGAATGTTGTA AAGAATGTTGTTGTCCAAGAATAAAAGCATTTAAGAAATTTATAAACACATTTGAAAAAGCACAAATTGG AAAAGAAGCACCAGAATTTAAAGCACCAGCATATTGTCCATGTGGTTCAATCAAAGAGATTGATATTAAT GAATATAGAGGAAAATATGTTGTATTGTTGTTTTATCCATTGGATTGGACATTTGTTTGTCCAACAGAAA TGATTGGATATAGTGAACTTGCAGGACAATTGAAAGAAATCAATTGTGAAGTTATTGGAGTGAGTGTAGA TTCAGTTTATTGTCATCAAGCATGGTGTGAAGCAGATAAAAGTAAAGGAGGAGTAGGAAAGTTGACATTC CCATTAGTATCAGATATTAAGAGATGCATTTCTATCAAATATGGAATGTTAAATGTCGAAGCAGGAATTG CAAGAAGAGGATATGTCATCATTGACGATAAAGGAAAAGTAAGATACATTCAAATGAATGATGATGGAAT TGGAAGATCAACGGAAGAAACAATCAGAATAGTGAAAGCAATTCAATTCAGTGATGAACATGGAGCAGTT TGTCCACTCAATTGGAAACCAGGCAAAGACACCATTGAACCAACACCAGATGGAATTAAGAAATATTTAA CAGCACATTAAAACAAACAAGATAATTTAATACAAATTATTTTATGTTTTATAAGAAGAAAATGATATAA TAAAAGATAAA >CAA50324.1 alkyl hydroperoxide reductase [Entamoeba histolytica] MSCNQQKECCKKECQEKECCKECCCPRIKAFKKFINTFEKAQIGKEAPEFKAPAYCPCGSIKEIDINEYR GKYVVLLFYPLDWTFVCPTEMIGYSELAGQLKEINCEVIGVSVDSVYCHQAWCEADKSKGGVGKLTFPLV SDIKRCISIKYGMLNVEAGIARRGYVIIDDKGKVRYIQMNDDGIGRSTEETIRIVKAIQFSDEHGAVCPL NWKPGKDTIEPTPDGIKKYLTAH Protective antigen 80% of C3H/HeJ mice immunized with Eh29 administered in combination with a subclinical dose of whole cholera toxin, but not as an Eh29-CTxB fusion, showed no evidence of infection in tissue sections harvested following intracecal challenge with virulent E. histolytica trophozoites. These results suggest that Eh29 is capable of inducing protective anti-amoebic immune responses in mice following oral immunization and could be used in the development of oral vaccines against amoebiasis [Ref1382:Carrero et al., 2010]. SREHP Entamoeba histolytica HM-1:IMSS VO_0011324 3402462 67463194 EHI_116360 DS571976 XP_648254 294381 Unknown 1107 1833 - 4.01 24419.56 233 transcript EHI_116360A >NW_001915691.1:1107-1833 Entamoeba histolytica HM-1:IMSS scf_1104750518053 genomic scaffold, whole genome shotgun sequence AGACTAAAGTCAAATAACTTCATTTAGAAGATGATAGCTATAATGATAGCACAGAAAACAATGAATGGAC TTGATGCAGCATCAAGGTTATTATTATCGTTATCTGAACTACTTCCTGATTTATCATTTGAATTACTAGT TGAGCTTGCTTCTGGTTTATTAGTTGAGCTTGCTTCTGGTTTATTAGTTGAGCTTGCTTCTGGTTTATTA GTTGAGCTTGCTTCTGGTTTATTAGTTGAGCTTGCTTCTGGTTTATTATCTGGTTTATCACTTGAGCTTG CTTCTGGTTTATTATCTGGTTTATCACTTGAGCTTGCTTCTGGTTTATTATCTGGTTTATCACTTGAACT TGCTTCTGGTTTATTATCTGGTTTATCACTTGAACTTGCTTCTGGTTTATTATCTGGTTTATCACTTGAA CTTGCTTCTGGTTTATCACTTGAACTTGCTTCTGGTTTATTATCTGGTTTATCACTTGAGCTTGATTCTG AGTTATCACTTGAACTTGCTTTTTCATCTTCATCATCTTCATTATCTTCATTTGAACTTGATTCTGGTTT TGCTGAGCTACTTTTTTCTTTTTCTTCAGCTTCTTCAAGCTTTTCAGGACTAGCTTCGTTCTTTAAAAAT ACACCGTAGATATTAGTATCTTTTACTTCTTGATCCAAATCAAGAATGATATTAGTTGCACTAGTGAATG CAATAAACAATAAAAATGCGAACATTG >XP_648254.1 serine-rich protein [Entamoeba histolytica HM-1:IMSS] MFAFLLFIAFTSATNIILDLDQEVKDTNIYGVFLKNEASPEKLEEAEEKEKSSSAKPESSSNEDNEDDED EKASSSDNSESSSSDKPDNKPEASSSDKPEASSSDKPDNKPEASSSDKPDNKPEASSSDKPDNKPEASSS DKPDNKPEASSSDKPDNKPEASSTNKPEASSTNKPEASSTNKPEASSTNKPEASSTSNSNDKSGSSSDND NNNLDAASSPFIVFCAIIIAIIF Protective antigen Report describes a recombinant fusion protein containing the serine-rich Entamoeba histolytica protein (SREHP), a protective antigen derived from virulent amebae, and a bacterially derived maltose-binding protein (MBP) from an attenuated strain of Salmonella typhimurium. Gerbils vaccinated with S typhimurium SREHP-MBP were protected against amebic liver abscess after challenge with E. histolytica, the most common extraintestinal complication of amebiasis [Ref1384:Zhang and Stanley, 1996]. Carrero et al., 2010 journal Carrero JC, Contreras-Rojas A, Sánchez-Hernández B, Petrosyan P, Bobes RJ, Ortiz-Ortiz L, Laclette JP 2010 Experimental parasitology He, 2012 journal He GZ 2012 130 2 126-129 Experimental parasitology Houpt et al., 2004 journal Houpt E, Barroso L, Lockhart L, Wright R, Cramer C, Lyerly D, Petri WA 2004 22 5-6 611-617 Vaccine Petri and Ravdin, 1991 journal Petri WA Jr, Ravdin JI 1991 59 1 97-9101 Infection and immunity Priest et al., 2010 journal Priest JW, Kwon JP, Montgomery JM, Bern C, Moss DM, Freeman AR, Jones CC, Arrowood MJ, Won KY, Lammie PJ, Gilman RH, Mead JR 2010 17 6 954-965 Clinical and vaccine immunology : CVI Wiki: Entamoeba histolytica website http://en.wikipedia.org/wiki/Entamoeba_histolytica Zhang and Stanley, 1996 journal Zhang T, Stanley SL Jr 1996 64 5 1526-1531 Infection and immunity