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VSG Signal sequence Amino-terminal domain Carboxy-terminal domain T. brucei MITat1.4 MDCHTKETLGVTQWRRSTMLTLSLLYAITPADG A | | | RHGTEADFDAGAGPAESEVADSGFAQVPGKQDGANAGQANM | | MITat1.2 MPSNQEARLFLAVLVLAQVLPILVDS A QVSEELDDQPKGALFTLQAAASKIQKMRDAALRASIYAEINHGTNRAKAAVIVANHYAMKADSGLEALKQTLSSQEVTATATASYLKGRIDEYLNLLLQTK| | | † SRA MPRNSGRTTSTLALAVALKLLAVPVSPSGT A | FDEEPVKKV † | | | † STAQTQKLKEKILNTLVPKLVEGSKSQVKLRILKYPGKIQKSKLVSIQELKTRVEPESST | MITat1.5 MIHSNKVATVVLALISSWPADG T KVEKNLADVAGIALAKINNLIKQVSAATEAEARMTLAAASTDHS | ISALYAAASNIVTR † | VLNAVHALTSLAPIALTAATNGAKTSGHISEVIDILQQASQGKTEGK † IVKSGGGTTTVAIRQLYNKIGDLEKQTTNN | | | | † HAAVKAAQDMKADPALKVDQTLLAVLVASPEMAEILKLEAAASQQKGPEEVTIDLATEKNNYFGTNNNKLEPLWTKIKGQNIVDLAATKGSTKELGTVTDTAELQKLLSYYYTVNKEEQKK MMDTSGTNTVTKAGGTIGGVP KLQLSPIQPKRPAATYLGKAGYVGLTRQADAANNFHDNDAE RLASGHNTNGLGKSGQLSAAVTMAAGYVTVANSQTAVTVQALDALQEASGAAHQPWIDAWKAKKALTGAET ETAGIAGKTGVTKLVEEALLKKKDSEASEIQTELKKYFSGHENEQWTAIEKLISEQPVAQNLVGDNQPTKLGELEGNAKLTTILAYYRMETAGKFEV KMSKELKATAMRAANDAKLKITEILELENVFAAMIP ATKGTEADG TDYNAVFLEA NTAAETVSKIATLAESATKAAGAAGRAAGVLDEFIAALAQAQGAT IQGSGTGAATHTELAD FNGDLKPRNMLSIRDPKVSAAATGSTDLTTLAKAMAASGTDTTFHGDQQSKG GLMKGTSDGIMIGQALTGTFAWAQGLLRFGALGANGIASTGVTGYAHTATASGNGVHWASDPEKIPVIAEAIALVSNYNTLADSIGTRAKDAI MKATNKEIKREHIFL VSHLNRELQKAVTELDKALNK NKISEEPK | | DDKKQIE † | KF STKAKEKGVSVTQTQTAGGTEATTDK| KGKLEDT | | | K NKKDQNE | | TLDKEEAKKVADETAKDGKTGNT† | | | | NAIGDDKDK KGKLEPG TKAQEYEWEGKESK | | | | TQHGTNKEA GFRKGKDGETDEPDKEK| ILTat1.25 MQSQQQPVFISIILLAINTDAA A | | | † | | L LOUTat1.5 MQQSRSRTPTCSKNCTLKALFITVATLILAPKTSD A | | | † | | L | | | | † DGSEANGKGS VILSTSASKYKVETPDWLNALEAAIADLEQEQIELDNGRKAEAQILAL EPTKQPPAKAAAAPEKKSNPQKD | | | | | QT DGSSTA A VYLGANGDAPNKP TWLDELTQALLAAQTAA PTTAVNAREFGLL TLVRAEDNLEDRRSAGQAAKEVVALAAKIELILANLKHIERLAAAEPEAAPKESRSDETPEA KASKATV SQAAQTYKTIRPDEKLALAFLAETTGDLRSTF VTLKQITAAAASHARYFGENTESRPALDKIKKALYGSPEAKGDAIIESGDGT GNTDGNAANSAAKRATAALI GGDNTNTGNDA FTQTTADINYAKKGGEVERAWTEIRQK KAGAAANKVTAAQLKAAAAELAALIHQKRGEKAVAGLLGAAQINND AAATAGSNSAVFQHL TLVNAVTEVEKVGDVPATVTQIHAIAERTALIFRAAKELEELAAQTPGTTKKEVAPKKPNTI TERLKDA DKAATYLKQMMPQDRQHLLAFVASSDPTVQLV DTANSLLLKTSNFIADAKKRSNKEVLKHLRTALYSEGKDSVTNAIFTATSGR GSQSGGAAKGAKNNLAATLL AGDSTN DNEAVPAVTFNKNGNDAASAFEKIRTI KRRAETPTLSRLPQAIAAAIGAVTADLAAPKGDNPDVGTIGGITTGGRPD SSXTTLLAQAV | | | | TWLDELTQALLAAQTAAKAELDSTAQAAHIEGI†TTLALALLNGIYQTQANSRQQTHQEAPQHPREHMANSAKT| EQHKGnKTA | | | | | EAKGGEDGVKAANDGKST†TTGN T. congo MIKVLLTLLSVAVCQKGLT S | † | | | | | † | | | GELDNVQEFGIL RIYQIASTTVPEASSAHDGQMTKLMKDISDIVLSTTA DSYYEAESTKITPNIKEH KRISASSQTQPLVRKMRRILARASARAAELGSLGKEDQSARDTIRKALLKAIYGKDVDTQEDGEAAVRGAEAPVFGDQKSKLGS GGSGGPSTGEHVGVSLVNDFF L IAGGHSAGDKW HISIAKASANKNWASLTGHDTEWGKIKTN PRFSV LTASAIDQALMAFHSRLGGGGKGTPNGDSGQQIGGYIFGKTGTLA TGDDGQV LNYKKNLVPESNGKIKGIDWEKRLREASWELRQIEERKREGEVLLTQLEMLNHSAW LEAWDRVEDER SSSTKVSGSPEGDKGTTKTPIS†GSLPI E AEGGNAAEFQLL DAARLAAAMATGKERSMLATTGSPESVARVEVGQGLIGAALEAWLNGQSDEADKKIAEETASRMTEASQTHSDALKAALTAAEAHARSQAQSKQAEAKKLAAQALGVDEGT LTITQSSTKGEQKWTSSAPASYA KTQAQNE LKGLVSSNDIAQNNAVEKWETDIKTRIDKP C T. vivax ..DWGGDNAENIGACSVWLLFARHAE | | | TTHAGKIAGDIMYL | | | LAGDHTGIEVTLDAVDTAIGRIRAAVGTKSGKDKFGSDSSTTLTYTAAFATNGNGNEGEHFWGKKLKQAATHLAQARQALAFAQEMQARKRKIENTERLVGDPLAETKTRRAAKEQTATEAQKRDHQ GNEDMSTRETGKK FIGURE 5.3 Conserved features of typical VSG sequences. VSG amino-terminal domains fall into two major classes, having either 4–6 or 10–12 cysteine residues (indicated by vertical bars). Carboxy-terminal subdomains contain two disulfide bonds and T. brucei or two subdomains. All seven sequenced T. congolense VSGs have a similar structure to the one example shown, but do not contain the carbo terminal subdomain found in T. brucei VSGs. The single known T. vivax VSG also lacks the carboxy-terminal domain and is distinguished b absence of N-glycosylation sites. Disulfide linkages have been experimentally determined for one T. brucei and one T. by the overlines) but cysteine residues are so highly conserved that they are likely to adopt the same pairing in all VSGs sequences indicate the boundary between amino- and carboxy-terminal domains, based on crystal structures or by carboxy-terminal signal sequences highlight the extraordinary conservation of VSG GPI signal sequences, where a br the hydrophobic domain, to emphasize the conserved bipartite motif. The carboxy-terminal GPI attachment sites have been exper determined for MITat 1.2, 1.4 & 1.5 and are predicted for the other sequences, which are highly conserved in T. congolense. The mature amino-termini were experimentally determined for all sequences except VSG ILTat1.25 and SRA, which w predicted using SignalP. † indicates probable N-glycosylation sites. These have been experimentally verified for MITat 1.2, 1.4 & 1.5. S N-glycosylation sites within disulfide-linked regions of carboxy-terminal subdomains of some VSGs are not marked as they ar cosylated, because of accessibility constraints. SRA is the VSG-like molecule that can confer human infectivity on T. brucei | | | | NKNTKKRD NEDKI GDTPG KEGDG SWHKEVKAGEKH| GWHKAEGK KWSSTEATEGAF NnETR EAKDGEGQKNQATGEKDANKNR| SYDDSKGSDKK KPKDGEGQTSAAGAGDAGASDTEAKK KSP TYNAEKAEANGAPATQPQGGVNEATTGN| TEAK | KWHNDAENKK EKENTPGQSAV SDKKKEEE KWKGGDDEKGE| KKESN KSPN | KWENNA KWDGKE TGS
96 ANTIGENIC VARIATION structures. The same is probably true of the smaller carboxy-terminal subdomains, which tend to have more-conserved sequences and appear to be very tightly folded. Interestingly, the few sequenced VSGs of T. congolense and T. vivax are quite distinct from those of T. brucei (Figure 5.3). They are smaller and lack any clear carboxy-terminal domain, which is probably relevant to assessing evolutionary relationships among the various African trypanosomes. VSG synthesis, processing, secretion and turnover Trypanosomes contain components of the conventional eukaryotic signal recognition machinery, and VSG contains an apparently conventional amino-terminal signal sequence, although there is published evidence that signal sequences are not so exchangeable as one might imagine. VSG is presumably synthesized on ribosomes that are bound to the endoplasmic reticulum, and the nascent polypeptide is translocated into the lumen of the endoplasmic reticulum, with co-translational cleavage of the amino-terminal signal sequence. Cleavage of the carboxy-terminal GPI signal sequence and covalent coupling of the pre-assembled core GPI anchor also appears to be a coupled and immediately post-translational event, concomitant with or prior to N-glycosylation. It has been proposed that the secondary glycosylation of the VSG-linked GPI anchor and N-linked glycans represents a ‘space-filling’ function, determined by the accessibility of the primary glycans to further glycosylation by Golgi-resident glycosyl-transferases, as VSG dimers traverse the secretory pathway. In trypanosomes engineered to express two VSGs simultaneously, the patterns of N-glycosylation and GPI glycosylation are almost identical to those found when each VSG is expressed individually in its normal cell background, which confirms that the overall structures of the VSG homodimers determine the extent and nature of the secondary glycan modifications, not the cell background in which they are expressed. VSG half-life is more than 30 h (about 5 cell generations), yet VSG is continually and rapidly recycled, in the absence or presence of specific antibody. It is not known whether a mechanism exists for more rapid removal of the ‘old’ VSG, during a VSG switch. The only recognized site of endo- and exocytosis in trypanosomes is the flagellar pocket, an invagination at the exit point of the flagellum, which accounts for a small part of the total surface membrane area but turns over at a high rate. Certain ‘cell-surface’ proteins appear to be specifically retained in the flagellar pocket by a mechanism that may depend on a unique glycosylation pattern recognized by hypothetical trans-membrane receptor lectins in the flagellar pocket. In the context of antigenic variation, the flagellar-pocket retention of the heterodimeric transferrin receptor is intriguing, as it is also GPI anchored, but only via one of the two subunits. The locations of the many other GPI-anchored and transmembrane proteins expressed by T. brucei are unknown. In recent years, much attention has been focused on the sorting of membrane proteins, with the recognition that cellular membranes are not lakes of randomly distributed lipids but consist of lipid-specific subdomains. The concept of lipid rafts has particular relevance to GPI-anchored proteins, and suggests that the very specific myristylation of the VSG GPI anchor is probably an important determinant of VSG secretion and recycling. T. brucei appears to exert a high degree of quality control on VSG secretion. Attempts to use bloodstream-form T. brucei to express high levels of alien GPIanchored proteins have failed. Even small modifications of VSG structure are deleterious to MOLECULAR BIOLOGY
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Molecular Medical Parasitology
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Molecular Medical Parasitology Edit
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Contents List of contributors Prefa
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List of contributors Mark Blaxter,
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LIST OF CONTRIBUTORS ix Richard. J.
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Preface Parasitology was born as th
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S E C T I O N I MOLECULAR BIOLOGY
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C H A P T E R 1 Parasite genomics M
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TABLE 1.1 Parasite genomes: genome
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GENERATING GENOMICS DATA 7 differen
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GENERATING GENOMICS DATA 9 TABLE 1.
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GENERATING GENOMICS DATA 11 called
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GENERATING GENOMICS DATA 13 200 000
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BIOINFORMATICS AND THE ANALYSIS OF
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THE POST-GENOMICS ERA, AND THE OTHE
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THE PARASITES AND THEIR GENOMES 19
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FURTHER READING 27 treated with a d
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C H A P T E R 2 RNA processing in p
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TRANS-SPLICING 31 cis trans Exon 1
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TRANS-SPLICING 33 snRNPs (small nuc
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TRANS-SPLICING 35 trans cis U2AF35
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RNA EDITING 37 P AAAA... AAAA... AA
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RNA EDITING 39 entire transcript re
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RNA EDITING 41 5 Editing block C Ed
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RNA EDITING 43 microscopy) approach
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Page 60 and 61: C H A P T E R 3 Transcription Arthu
Page 62 and 63: UNUSUAL MODES OF TRANSCRIPTION IN T
Page 64 and 65: CLASS I TRANSCRIPTION IN TRYPANOSOM
Page 70 and 71: CLASS II TRANSCRIPTION OF PROTEIN C
Page 72 and 73: SL RNA AND U snRNA GENE TRANSCRIPTI
Page 78 and 79: FURTHER READING 65 and switching in
Page 80 and 81: C H A P T E R 4 Post-transcriptiona
Page 82 and 83: POST-TRANSCRIPTIONAL REGULATION IN
Page 100 and 101: FURTHER READING 87 inhibition, it m
Page 102 and 103: C H A P T E R 5 Antigenic variation
Page 104 and 105: ANTIGENIC VARIATION AT THE STRUCTUR
Page 106 and 107: ANTIGENIC VARIATION AT THE STRUCTUR
Page 110 and 111: GENETICS OF ANTIGENIC VARIATION 97
Page 116 and 117: IMMUNE RESPONSES TO TRYPANOSOME INF
Page 118 and 119: INNATE RESISTANCE, HUMAN SUSCEPTIBI
Page 120 and 121: ANTIGENIC VARIATION IN MALARIA 107
Page 122 and 123: FURTHER READING 109 ACKNOWLEDGEMENT
Page 124 and 125: C H A P T E R 6 Genetic and genomic
Page 126 and 127: ‘FORWARD’ VS. ‘REVERSE’ GEN
Page 128 and 129: EXAMPLES OF ‘FORWARD’ GENETIC A
Page 130 and 131: EXAMPLES OF ‘FORWARD’ GENETIC A
Page 132 and 133: REVERSE GENETICS AND LEISHMANIA VIR
Page 134 and 135: VALIDATION OF CANDIDATE VIRULENCE G
Page 136 and 137: S E C T I O N II BIOCHEMISTRY AND C
Page 138 and 139: C H A P T E R 7 Energy metabolism P
Page 140 and 141: SUBCELLULAR ORGANIZATION OF AMITOCH
Page 142 and 143: CELL MEMBRANE Fructose [b] Glucose
Page 144 and 145: STEPS OF AMITOCHONDRIATE CORE METAB
Page 146 and 147: ENZYMATIC DIFFERENCES BETWEEN AMITO
Page 148 and 149: ACTION OF NITROIMIDAZOLE DRUGS 135
Page 150 and 151: ENVOI 137 unambiguously reflect the
Page 152 and 153: FURTHER READING 139 Saavedra-Lira,
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Page 156 and 157: THE EMBDEN-MEYERHOF-PARNAS (EMP) PA
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THE EMBDEN-MEYERHOF-PARNAS (EMP) PA
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WHY DO TRYPANOSOMATIDAE HAVE GLYCOS
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FURTHER READING 153 for use in agri
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CARBOHYDRATE METABOLISM 155 as a hu
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158 ENERGY METABOLISM - APICOMPLEXA
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172 PROTEIN METABOLISM PROTEINS (1)
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174 PROTEIN METABOLISM the C-termin
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176 PROTEIN METABOLISM and also, to
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178 PROTEIN METABOLISM values rangi
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180 PROTEIN METABOLISM of the plasm
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182 PROTEIN METABOLISM in vivo, in
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184 PROTEIN METABOLISM PROLINE Poly
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186 PROTEIN METABOLISM CO 2 Dec-SAM
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188 PROTEIN METABOLISM a cMDH has b
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190 PROTEIN METABOLISM Urea ARGININ
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192 PROTEIN METABOLISM been describ
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194 PROTEIN METABOLISM absence of g
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198 PURINES AND PYRIMIDINES enable
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200 PURINES AND PYRIMIDINES provide
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202 PURINES AND PYRIMIDINES activit
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204 PURINES AND PYRIMIDINES physiol
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206 PURINES AND PYRIMIDINES Amitoch
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208 PURINES AND PYRIMIDINES their a
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210 PURINES AND PYRIMIDINES FIGURE
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214 PURINES AND PYRIMIDINES protein
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220 PURINES AND PYRIMIDINES in Plas
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222 PURINES AND PYRIMIDINES whereas
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226 TRYPANOSOMATID CARBOHYDRATES AF
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228 TRYPANOSOMATID CARBOHYDRATES In
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230 TRYPANOSOMATID CARBOHYDRATES po
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232 TRYPANOSOMATID CARBOHYDRATES LP
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234 TRYPANOSOMATID CARBOHYDRATES re
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236 TRYPANOSOMATID CARBOHYDRATES sc
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A. sAP COOH [T][T](S/T)(S/T)(S/T)SS
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240 TRYPANOSOMATID CARBOHYDRATES Cr
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242 INTRACELLULAR SIGNALING protein
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244 INTRACELLULAR SIGNALING FIGURE
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246 INTRACELLULAR SIGNALING 212.5 2
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248 INTRACELLULAR SIGNALING cycle.
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250 INTRACELLULAR SIGNALING V-H -A
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252 INTRACELLULAR SIGNALING domain)
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254 INTRACELLULAR SIGNALING the kno
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256 INTRACELLULAR SIGNALING from in
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258 INTRACELLULAR SIGNALING FIGURE
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260 INTRACELLULAR SIGNALING ESAG4 (
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262 INTRACELLULAR SIGNALING and ind
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264 INTRACELLULAR SIGNALING ATPase
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266 INTRACELLULAR SIGNALING G11XG
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268 INTRACELLULAR SIGNALING a diffe
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270 INTRACELLULAR SIGNALING rapid l
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272 INTRACELLULAR SIGNALING cells w
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274 INTRACELLULAR SIGNALING PfPPJ i
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276 INTRACELLULAR SIGNALING is cont
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278 PLASTIDS, MITOCHONDRIA, AND HYD
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298 HELMINTH SURFACES Important exc
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300 HELMINTH SURFACES protease inhi
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302 HELMINTH SURFACES volume, there
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304 HELMINTH SURFACES projecting si
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306 HELMINTH SURFACES schistosome t
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308 HELMINTH SURFACES re-establish
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310 HELMINTH SURFACES hepatic cells
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312 HELMINTH SURFACES lungs. Larvae
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314 HELMINTH SURFACES cuticle, whic
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316 HELMINTH SURFACES cuticle in th
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318 HELMINTH SURFACES mec-8 or sym-
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320 HELMINTH SURFACES current, when
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322 HELMINTH SURFACES The cuticle-h
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324 HELMINTH SURFACES are typically
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326 HELMINTH SURFACES or carrier pr
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328 HELMINTH SURFACES of tyrosine-b
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330 HELMINTH SURFACES blood. The ge
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332 HELMINTH SURFACES Mutations in
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334 HELMINTH SURFACES in the hypode
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336 HELMINTH SURFACES (including H-
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338 HELMINTH SURFACES Blaxter, M.L.
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340 ENERGY METABOLISM IN HELMINTHS
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360 NEUROTRANSMITTERS CO 2 H NH 2 G
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362 NEUROTRANSMITTERS TABLE 15.1 An
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364 NEUROTRANSMITTERS more arms tha
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366 NEUROTRANSMITTERS the surroundi
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368 NEUROTRANSMITTERS proteins requ
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370 NEUROTRANSMITTERS FIGURE 15.11
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372 NEUROTRANSMITTERS FIGURE 15.13
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374 NEUROTRANSMITTERS sensitivity t
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376 NEUROTRANSMITTERS TABLE 15.3 Cl
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378 NEUROTRANSMITTERS crossed the c
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380 NEUROTRANSMITTERS have been tes
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382 NEUROTRANSMITTERS C-terminals a
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384 NEUROTRANSMITTERS Davis and Str
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386 NEUROTRANSMITTERS Cephalic gang
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388 NEUROTRANSMITTERS myoexcitation
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390 NEUROTRANSMITTERS is phosphoryl
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392 NEUROTRANSMITTERS many other an
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398 DRUG RESISTANCE of some of the
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400 DRUG RESISTANCE It is now estim
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402 DRUG RESISTANCE is again assume
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404 DRUG RESISTANCE An alternative
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406 DRUG RESISTANCE clinical eviden
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408 DRUG RESISTANCE FIGURE 16.4 Fol
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410 DRUG RESISTANCE Using similar s
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412 DRUG RESISTANCE whether these r
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414 DRUG RESISTANCE FIGURE 16.5 Str
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416 DRUG RESISTANCE FIGURE 16.6 Try
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418 DRUG RESISTANCE has permitted e
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420 DRUG RESISTANCE FIGURE 16.7 Dru
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422 DRUG RESISTANCE near future. Th
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424 DRUG RESISTANCE million new inf
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426 DRUG RESISTANCE some 50 million
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428 DRUG RESISTANCE pharynx, the bo
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430 DRUG RESISTANCE efforts for glo
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432 DRUG RESISTANCE and resistance
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434 MEDICAL IMPLICATIONS TABLE 17.1
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436 MEDICAL IMPLICATIONS TABLE 17.1
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438 MEDICAL IMPLICATIONS transmissi
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440 MEDICAL IMPLICATIONS H 2 C H H
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442 MEDICAL IMPLICATIONS parasites
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444 MEDICAL IMPLICATIONS neuropsych
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446 MEDICAL IMPLICATIONS of toxic f
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448 MEDICAL IMPLICATIONS Future con
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450 MEDICAL IMPLICATIONS Melarsopro
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452 MEDICAL IMPLICATIONS prevention
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454 MEDICAL IMPLICATIONS resulting
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456 MEDICAL IMPLICATIONS for S. ste
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458 MEDICAL IMPLICATIONS are though
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460 MEDICAL IMPLICATIONS FIGURE 17.
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462 MEDICAL IMPLICATIONS Marr, J.J.
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464 INDEX Aldolase, 143 Plasmodium
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466 INDEX Ascofuranone, 143 ASCUT-1
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468 INDEX Cnidarians, RNA trans-spl
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470 INDEX Entamoeba, 125 Ca 2 metab
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472 INDEX Glucose-6-phosphate dehyd
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474 INDEX Ivermectin, 398, 427, 455
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476 INDEX Maduramicin, 412 Major va
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478 INDEX Nitric oxide: neurotransm
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480 INDEX calcium-binding proteins,
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482 INDEX Pyrimidine transport, 200
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484 INDEX Succinate:rhodoquinone ox
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486 INDEX genome, 21 survey sequenc
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488 INDEX U small nuclear RNA (snRN
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