The complete amino acid sequence of human complement factor H

Ripoche, Jean; Day, Anthony J.; Harris, Tim; Sim, Robert B.

doi:10.1042/bj2490593

Cited by 326 publications

(261 citation statements)

References 26 publications

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“…Primers for PCR were made based on the sequence of the H cDNA [27] These were used to amplify a 130 bp fragment from genomic DNA. This fragment was subsequently cloned into the Eco RI site of pUC18 and DNA from a single colony was isolated and sequenced.…”

Section: Cloning and Sequencing The Promoter Region Of The Human H Genementioning

confidence: 99%

“…The RNA was transferred to nylon membranes and the blots probed sequentially with human factor H and actin. The factor H cDNA probe used was a 0.7 kb fragment representing positions 750-1425 of the published cDNA sequence, which identified a 4.5 kb mRNA [27]. The actin probe was a cDNA fragment of chicken actin [32].…”

Section: Cloning and Sequencing The Promoter Region Of The Human H Genementioning

confidence: 99%

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Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Williams

Vik

1997

Scand J Immunol

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Williams SA, Vik DP. Characterization of the 5 0 Flanking Region of the Human Complement Factor H Gene. Scand J Immunol 1997;45:7-15 The promoter region of the human factor H gene was cloned and a 3 kb Eco RI fragment was sequenced. Primer extension and S1 nuclease analysis were used to determine the transcription start site, which was found to be 10-11 nucleotides upstream of the published cDNA sequence. No canonical TATA or CCAAT boxes were found in conjunction with this site. The sequence from the human H promoter region was compared to that from the mouse gene. There was a region of 800 bp that was 62.5% identical between the two sequences. The sequences of the two promoter regions were compared to a database of transcription factor binding sites. Five elements were identified that matched the consensus sequence 100% and were identical in the two promoter sequences. Promoter assays using the luciferase reporter gene demonstrated that this region contained a functional transcription start site and putative enhancer elements. U118-MG astroglioma cells and Hep3b hepatoma cells were incubated with various cytokines to measure effects on their factor H mRNA levels. Interferon-(IFN-), but not interleukin-1 (IL-1), tumour necrosis factor (TNF-) or IL-6, was able to increase the level of H mRNA in both cell lines.

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Section: Cloning and Sequencing The Promoter Region Of The Human H Genementioning

confidence: 99%

Section: Cloning and Sequencing The Promoter Region Of The Human H Genementioning

confidence: 99%

Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Williams

Vik

1997

Scand J Immunol

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“…It is a glycoprotein in human plasma composed of 20 repetitive units of 60 aa, which is designated complement control protein domains or short consensus repeats (SCRs) (20). Another regulator of the alternative pathway is the FHL-1, which is a product of alternative splicing of the FH gene (21).…”

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confidence: 99%

Haemophilus influenzae Interacts with the Human Complement Inhibitor Factor H

Hallström

Zipfel

Blom

et al. 2008

The Journal of Immunology

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Pathogenic microbes acquire human complement inhibitors to circumvent the innate immune system. In this study, we identify two novel host-pathogen interactions, factor H (FH) and factor H-like protein 1 (FHL-1), the inhibitors of the alternative pathway that binds to Hib. A collection of clinical Haemophilus influenzae isolates was tested and the majority of encapsulated and unencapsulated bound FH. The isolate Hib 541 with a particularly high FH-binding was selected for detailed analysis. An increased survival in normal human serum was observed with Hib 541 as compared with the low FH-binding Hib 568. Interestingly, two binding domains were identified within FH; one binding site common to both FH and FHL-1 was located in the N-terminal short consensus repeat domains 6–7, whereas the other, specific for FH, was located in the C-terminal short consensus repeat domains 18–20. Importantly, both FH and FHL-1, when bound to the surface of Hib 541, retained cofactor activity as determined by analysis of C3b degradation. Two H. influenzae outer membrane proteins of ∼32 and 40 kDa were detected with radiolabeled FH in Far Western blot. Taken together, in addition to interactions with the classical, lectin, and terminal pathways, H. influenzae interferes with the alternative complement activation pathway by binding FH and FHL-1, and thereby reducing the complement-mediated bactericidal activity resulting in an increased survival. In contrast to incubation with active complement, H. influenzae had a reduced survival in FH-depleted human serum, thus demonstrating that FH mediates a protective role at the bacterial surface.

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“…Although the function of these cysteine-rich motifs remains unclear, one speculation is that they play a role in the stabilization of ␤-turns that are presumably involved in protein-protein interactions (3). In addition, the carboxyl termini of C6, factors H and I, also have cysteine-rich motifs (termed factor I domains), and this domain has been implicated in the capacity of these proteins to specifically interact with C5 (25)(26)(27).…”

Section: Discussionmentioning

confidence: 99%

Isolation, Characterization, and Cloning of Porcine Complement Component C7

Agah

Montalto

Kiesecker

et al. 2000

The Journal of Immunology

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Activation of the complement system through the classical, alternative, or lectin pathway results in the formation of the terminal complement complex. C7 plays an integral role in the assembly of this complex with target cell membranes. To date, only human C7 has been cloned and characterized; thus, in this study, we characterized the porcine complement component C7. Porcine C7 was isolated by affinity chromatography as a single glycoprotein with an approximate molecular mass of 90 kDa and 100 kDa under reducing and nonreducing conditions, respectively. The full-length porcine C7 cDNA was isolated, and the predicted amino acid sequence exhibited 80% identity with human C7 with conservation of the cysteine backbone and two putative N-linked glycosylation sites. Porcine C7 mRNA expression was detected in all tissues investigated, except polymorphonuclear and mononuclear leukocytes. Addition of purified porcine C7 restored the hemolytic activity of C7-depleted human sera in a dose-dependent manner. A functionally inhibitory mAb against porcine C7 attenuated the hemolytic activity of human, rabbit, or rat sera, suggesting an important conserved C7 epitope among species. These data demonstrate that porcine and human C7 are highly conserved, sharing structural and functional characteristics.

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The complete amino acid sequence of human complement factor H

Cited by 326 publications

References 26 publications

Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Haemophilus influenzae Interacts with the Human Complement Inhibitor Factor H

Isolation, Characterization, and Cloning of Porcine Complement Component C7

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